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Volumn 85, Issue 6, 2012, Pages 1029-1043

Direct binding targets of the stringent response alarmone (p)ppGpp

Author keywords

[No Author keywords available]

Indexed keywords

ALARMONE; AMINO ACID DECARBOXYLASE; GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; RNA POLYMERASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR DKSA; UNCLASSIFIED DRUG;

EID: 84866038398     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08177.x     Document Type: Article
Times cited : (137)

References (129)
  • 1
    • 0030587932 scopus 로고    scopus 로고
    • An alpha to beta conformational switch in EF-Tu
    • Abel, K., Yoder, M.D., Hilgenfeld, R., and Jurnak, F. (1996) An alpha to beta conformational switch in EF-Tu. Structure 4: 1153-1159.
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 2
    • 33744457284 scopus 로고    scopus 로고
    • p)ppGpp regulates type 1 fimbriation of Escherichia coli by modulating the expression of the site-specific recombinase FimB
    • Aberg, A., Shingler, V., and Balsalobre, C. (2006) p)ppGpp regulates type 1 fimbriation of Escherichia coli by modulating the expression of the site-specific recombinase FimB. Mol Microbiol 60: 1520-1533.
    • (2006) Mol Microbiol , vol.60 , pp. 1520-1533
    • Aberg, A.1    Shingler, V.2    Balsalobre, C.3
  • 3
    • 33746826565 scopus 로고    scopus 로고
    • Origin of exopolyphosphatase processivity: fusion of an ASKHA phosphotransferase and a cyclic nucleotide phosphodiesterase homolog
    • Alvarado, J., Ghosh, A., Janovitz, T., Jauregui, A., Hasson, M.S., and Sanders, D.A. (2006) Origin of exopolyphosphatase processivity: fusion of an ASKHA phosphotransferase and a cyclic nucleotide phosphodiesterase homolog. Structure 14: 1263-1272.
    • (2006) Structure , vol.14 , pp. 1263-1272
    • Alvarado, J.1    Ghosh, A.2    Janovitz, T.3    Jauregui, A.4    Hasson, M.S.5    Sanders, D.A.6
  • 4
    • 0023711405 scopus 로고
    • Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12
    • Andrews, S.C., and Guest, J.R. (1988) Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12. Biochem J 255: 35-43.
    • (1988) Biochem J , vol.255 , pp. 35-43
    • Andrews, S.C.1    Guest, J.R.2
  • 5
    • 0032408864 scopus 로고    scopus 로고
    • The HD domain defines a new superfamily of metal-dependent phosphohydrolases
    • Aravind, L., and Koonin, E.V. (1998) The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem Sci 23: 469-472.
    • (1998) Trends Biochem Sci , vol.23 , pp. 469-472
    • Aravind, L.1    Koonin, E.V.2
  • 6
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind, L., and Koonin, E.V. (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J Mol Biol 287: 1023-1040.
    • (1999) J Mol Biol , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 8
    • 79961217635 scopus 로고    scopus 로고
    • The RelA/SpoT homolog (RSH) superfamily: distribution and functional evolution of ppGpp synthetases and hydrolases across the tree of life
    • Atkinson, G.C., Tenson, T., and Hauryliuk, V. (2011) The RelA/SpoT homolog (RSH) superfamily: distribution and functional evolution of ppGpp synthetases and hydrolases across the tree of life. PLoS ONE 6: e23479.
    • (2011) PLoS ONE , vol.6
    • Atkinson, G.C.1    Tenson, T.2    Hauryliuk, V.3
  • 9
    • 0035951301 scopus 로고    scopus 로고
    • Mechanism of regulation of transcription initiation by ppGpp. II. Models for positive control based on properties of RNAP mutants and competition for RNAP
    • Barker, M.M., Gaal, T., and Gourse, R.L. (2001a) Mechanism of regulation of transcription initiation by ppGpp. II. Models for positive control based on properties of RNAP mutants and competition for RNAP. J Mol Biol 305: 689-702.
    • (2001) J Mol Biol , vol.305 , pp. 689-702
    • Barker, M.M.1    Gaal, T.2    Gourse, R.L.3
  • 10
    • 0035951305 scopus 로고    scopus 로고
    • Mechanism of regulation of transcription initiation by ppGpp. I. Effects of ppGpp on transcription initiation in vivo and in vitro
    • Barker, M.M., Gaal, T., Josaitis, C.A., and Gourse, R.L. (2001b) Mechanism of regulation of transcription initiation by ppGpp. I. Effects of ppGpp on transcription initiation in vivo and in vitro. J Mol Biol 305: 673-688.
    • (2001) J Mol Biol , vol.305 , pp. 673-688
    • Barker, M.M.1    Gaal, T.2    Josaitis, C.A.3    Gourse, R.L.4
  • 11
    • 33750479525 scopus 로고    scopus 로고
    • Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism
    • Battesti, A., and Bouveret, E. (2006) Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism. Mol Microbiol 62: 1048-1063.
    • (2006) Mol Microbiol , vol.62 , pp. 1048-1063
    • Battesti, A.1    Bouveret, E.2
  • 12
    • 33751075737 scopus 로고    scopus 로고
    • Cooperative and critical roles for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA
    • Bharat, A., Jiang, M., Sullivan, S.M., Maddock, J.R., and Brown, E.D. (2006) Cooperative and critical roles for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA. J Bacteriol 188: 7992-7996.
    • (2006) J Bacteriol , vol.188 , pp. 7992-7996
    • Bharat, A.1    Jiang, M.2    Sullivan, S.M.3    Maddock, J.R.4    Brown, E.D.5
  • 13
    • 32344447009 scopus 로고    scopus 로고
    • The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme
    • Bilder, P., Lightle, S., Bainbridge, G., Ohren, J., Finzel, B., Sun, F., etal. (2006) The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45: 1712-1722.
    • (2006) Biochemistry , vol.45 , pp. 1712-1722
    • Bilder, P.1    Lightle, S.2    Bainbridge, G.3    Ohren, J.4    Finzel, B.5    Sun, F.6
  • 14
    • 34547913090 scopus 로고    scopus 로고
    • ppGpp regulation of RpoS degradation via anti-adaptor protein IraP
    • Bougdour, A., and Gottesman, S. (2007) ppGpp regulation of RpoS degradation via anti-adaptor protein IraP. Proc Natl Acad Sci USA 104: 12896-12901.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12896-12901
    • Bougdour, A.1    Gottesman, S.2
  • 15
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A., and McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 16
    • 38949175701 scopus 로고    scopus 로고
    • Feedback control of ribosome function in Escherichia coli
    • Bremer, H., and Dennis, P. (2008) Feedback control of ribosome function in Escherichia coli. Biochimie 90: 493-499.
    • (2008) Biochimie , vol.90 , pp. 493-499
    • Bremer, H.1    Dennis, P.2
  • 17
    • 32044468906 scopus 로고    scopus 로고
    • Conserved P-loop GTPases of unknown function in bacteria: an emerging and vital ensemble in bacterial physiology
    • Brown, E.D. (2005) Conserved P-loop GTPases of unknown function in bacteria: an emerging and vital ensemble in bacterial physiology. Biochem Cell Biol 83: 738-746.
    • (2005) Biochem Cell Biol , vol.83 , pp. 738-746
    • Brown, E.D.1
  • 18
    • 38749142232 scopus 로고    scopus 로고
    • Characterization of Nucleotide Pools as a Function of Physiological State in Escherichia coli
    • Buckstein, M.H., He, J., and Rubin, H. (2007) Characterization of Nucleotide Pools as a Function of Physiological State in Escherichia coli. J Bacteriol 190: 718-726.
    • (2007) J Bacteriol , vol.190 , pp. 718-726
    • Buckstein, M.H.1    He, J.2    Rubin, H.3
  • 19
    • 0036849768 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Obg GTP binding protein
    • Buglino, J., Shen, V., Hakimian, P., and Lima, C.D. (2002) Structural and biochemical analysis of the Obg GTP binding protein. Structure 10: 1581-1592.
    • (2002) Structure , vol.10 , pp. 1581-1592
    • Buglino, J.1    Shen, V.2    Hakimian, P.3    Lima, C.D.4
  • 20
    • 0038352105 scopus 로고    scopus 로고
    • Function of the universally conserved bacterial GTPases
    • Caldon, C.E., and March, P.E. (2003) Function of the universally conserved bacterial GTPases. Curr Opin Microbiol 6: 135-139.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 135-139
    • Caldon, C.E.1    March, P.E.2
  • 22
    • 0036069537 scopus 로고    scopus 로고
    • Gene expression profiling of Escherichia coli growth transitions: an expanded stringent response model
    • Chang, D.E., Smalley, D.J., and Conway, T. (2002) Gene expression profiling of Escherichia coli growth transitions: an expanded stringent response model. Mol Microbiol 45: 289-306.
    • (2002) Mol Microbiol , vol.45 , pp. 289-306
    • Chang, D.E.1    Smalley, D.J.2    Conway, T.3
  • 24
    • 0037125960 scopus 로고    scopus 로고
    • YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics
    • Daigle, D.M., Rossi, L., Berghuis, A.M., Aravind, L., Koonin, E.V., and Brown, E.D. (2002) YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. Biochemistry 41: 11109-11117.
    • (2002) Biochemistry , vol.41 , pp. 11109-11117
    • Daigle, D.M.1    Rossi, L.2    Berghuis, A.M.3    Aravind, L.4    Koonin, E.V.5    Brown, E.D.6
  • 26
    • 10344265937 scopus 로고    scopus 로고
    • Control of rRNA synthesis in Escherichia coli: a systems biology approach
    • Dennis, P.P., Ehrenberg, M., and Bremer, H. (2004) Control of rRNA synthesis in Escherichia coli: a systems biology approach. Microbiol Mol Biol Rev 68: 639-668.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 639-668
    • Dennis, P.P.1    Ehrenberg, M.2    Bremer, H.3
  • 27
    • 0017727849 scopus 로고
    • Regulation of ADP-glucose synthetase, the rate-limiting enzyme of bacterial glycogen synthesis, by the pleiotropic nucleotides ppGpp and pppGpp
    • Dietzler, D.N., and Leckie, M.P. (1977) Regulation of ADP-glucose synthetase, the rate-limiting enzyme of bacterial glycogen synthesis, by the pleiotropic nucleotides ppGpp and pppGpp. Biochem Biophys Res Commun 77: 1459-1467.
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 1459-1467
    • Dietzler, D.N.1    Leckie, M.P.2
  • 28
    • 0022495417 scopus 로고
    • Elongation factor Tu.guanosine 3′-diphosphate 5′-diphosphate complex increases the fidelity of proofreading in protein biosynthesis: mechanism for reducing translational errors introduced by amino acid starvation
    • Dix, D.B., and Thompson, R.C. (1986) Elongation factor Tu.guanosine 3′-diphosphate 5′-diphosphate complex increases the fidelity of proofreading in protein biosynthesis: mechanism for reducing translational errors introduced by amino acid starvation. Proc Natl Acad Sci USA 83: 2027-2031.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2027-2031
    • Dix, D.B.1    Thompson, R.C.2
  • 29
    • 38649092391 scopus 로고    scopus 로고
    • Transcription profiling of the stringent response in Escherichia coli
    • Durfee, T., Hansen, A.M., Zhi, H., Blattner, F.R., and Jin, D.J. (2008) Transcription profiling of the stringent response in Escherichia coli. J Bacteriol 190: 1084-1096.
    • (2008) J Bacteriol , vol.190 , pp. 1084-1096
    • Durfee, T.1    Hansen, A.M.2    Zhi, H.3    Blattner, F.R.4    Jin, D.J.5
  • 30
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 31
    • 0032924515 scopus 로고    scopus 로고
    • Effect of ppGpp on Escherichia coli cyclopropane fatty acid synthesis is mediated through the RpoS sigma factor (sigmaS)
    • Eichel, J., Chang, Y.Y., Riesenberg, D., and Cronan, J.E., Jr (1999) Effect of ppGpp on Escherichia coli cyclopropane fatty acid synthesis is mediated through the RpoS sigma factor (sigmaS). J Bacteriol 181: 572-576.
    • (1999) J Bacteriol , vol.181 , pp. 572-576
    • Eichel, J.1    Chang, Y.Y.2    Riesenberg, D.3    Cronan Jr., J.E.4
  • 33
    • 0017671547 scopus 로고
    • Biochemical mechanism of uracil uptake regulation in Escherichia coli B. Allosteric effects on uracil phosphoribosyltransferase under stringent conditions
    • Fast, R., and Skold, O. (1977) Biochemical mechanism of uracil uptake regulation in Escherichia coli B. Allosteric effects on uracil phosphoribosyltransferase under stringent conditions. J Biol Chem 252: 7620-7624.
    • (1977) J Biol Chem , vol.252 , pp. 7620-7624
    • Fast, R.1    Skold, O.2
  • 34
    • 58149142958 scopus 로고    scopus 로고
    • The stringent response and cell cycle arrest in Escherichia coli
    • Ferullo, D.J., and Lovett, S.T. (2008) The stringent response and cell cycle arrest in Escherichia coli. PLoS Genet 4: e1000300.
    • (2008) PLoS Genet , vol.4
    • Ferullo, D.J.1    Lovett, S.T.2
  • 35
    • 0015240172 scopus 로고
    • The mechanism of amino acid control of guanylate and adenylate biosynthesis
    • Gallant, J., Irr, J., and Cashel, M. (1971) The mechanism of amino acid control of guanylate and adenylate biosynthesis. J Bio Chem 246: 5812-5816.
    • (1971) J Bio Chem , vol.246 , pp. 5812-5816
    • Gallant, J.1    Irr, J.2    Cashel, M.3
  • 36
    • 34249323754 scopus 로고    scopus 로고
    • RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors
    • Gao, H., Zhou, Z., Rawat, U., Huang, C., Bouakaz, L., Wang, C., etal. (2007) RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors. Cell 129: 929-941.
    • (2007) Cell , vol.129 , pp. 929-941
    • Gao, H.1    Zhou, Z.2    Rawat, U.3    Huang, C.4    Bouakaz, L.5    Wang, C.6
  • 37
    • 0029069592 scopus 로고
    • Cellular localization of the Escherichia coli SpoT protein
    • Gentry, D.R., and Cashel, M. (1995) Cellular localization of the Escherichia coli SpoT protein. J Bacteriol 177: 3890-3893.
    • (1995) J Bacteriol , vol.177 , pp. 3890-3893
    • Gentry, D.R.1    Cashel, M.2
  • 38
    • 0027139270 scopus 로고
    • Synthesis of the stationary-phase sigma factor sigma s is positively regulated by ppGpp
    • Gentry, D.R., Hernandez, V.J., Nguyen, L.H., Jensen, D.B., and Cashel, M. (1993) Synthesis of the stationary-phase sigma factor sigma s is positively regulated by ppGpp. J Bacteriol 175: 7982-7989.
    • (1993) J Bacteriol , vol.175 , pp. 7982-7989
    • Gentry, D.R.1    Hernandez, V.J.2    Nguyen, L.H.3    Jensen, D.B.4    Cashel, M.5
  • 39
    • 0018600265 scopus 로고
    • Inosine 5′-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate
    • Gilbert, H.J., Lowe, C.R., and Drabble, W.T. (1979) Inosine 5′-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5′-monophosphate. Biochem J 183: 481-494.
    • (1979) Biochem J , vol.183 , pp. 481-494
    • Gilbert, H.J.1    Lowe, C.R.2    Drabble, W.T.3
  • 40
    • 0033403489 scopus 로고    scopus 로고
    • The intrinsic resistance of Escherichia coli to various antimicrobial agents requires ppGpp and sigma s
    • Greenway, D.L., and England, R.R. (1999) The intrinsic resistance of Escherichia coli to various antimicrobial agents requires ppGpp and sigma s. Lett Appl Microbiol 29: 323-326.
    • (1999) Lett Appl Microbiol , vol.29 , pp. 323-326
    • Greenway, D.L.1    England, R.R.2
  • 41
    • 0036084604 scopus 로고    scopus 로고
    • Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase
    • Guddat, L.W., Vos, S., Martin, J.L., Keough, D.T., and de Jersey, J. (2002) Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase. Protein Sci 11: 1626-1638.
    • (2002) Protein Sci , vol.11 , pp. 1626-1638
    • Guddat, L.W.1    Vos, S.2    Martin, J.L.3    Keough, D.T.4    de Jersey, J.5
  • 42
    • 0036192462 scopus 로고    scopus 로고
    • The universal stress protein paralogues of Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage
    • Gustavsson, N., Diez, A., and Nystrom, T. (2002) The universal stress protein paralogues of Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage. Mol Microbiol 43: 107-117.
    • (2002) Mol Microbiol , vol.43 , pp. 107-117
    • Gustavsson, N.1    Diez, A.2    Nystrom, T.3
  • 43
    • 0016250916 scopus 로고
    • Guanine nucleotides in protein synthesis. Utilization of pppGpp and dGTP by initiation factor 2 and elongation factor Tu
    • Hamel, E., and Cashel, M. (1974) Guanine nucleotides in protein synthesis. Utilization of pppGpp and dGTP by initiation factor 2 and elongation factor Tu. Arch Biochem Biophys 162: 293-300.
    • (1974) Arch Biochem Biophys , vol.162 , pp. 293-300
    • Hamel, E.1    Cashel, M.2
  • 44
    • 0021099181 scopus 로고
    • Guanosine 5′-triphosphate, 3′-diphosphate 5′-phosphohydrolase. Purification and substrate specificity
    • Hara, A., and Sy, J. (1983) Guanosine 5′-triphosphate, 3′-diphosphate 5′-phosphohydrolase. Purification and substrate specificity. J Biol Chem 258: 1678-1683.
    • (1983) J Biol Chem , vol.258 , pp. 1678-1683
    • Hara, A.1    Sy, J.2
  • 45
    • 0015221165 scopus 로고
    • Formation of ppGpp in a relaxed and stringent strain of Escherichia coli during diauxie lag
    • Harshman, R.B., and Yamazaki, H. (1971) Formation of ppGpp in a relaxed and stringent strain of Escherichia coli during diauxie lag. Biochemistry 10: 3980-3982.
    • (1971) Biochemistry , vol.10 , pp. 3980-3982
    • Harshman, R.B.1    Yamazaki, H.2
  • 46
    • 0015507370 scopus 로고
    • MSI accumulation induced by sodium chloride
    • Harshman, R.B., and Yamazaki, H. (1972) MSI accumulation induced by sodium chloride. Biochemistry 11: 615-618.
    • (1972) Biochemistry , vol.11 , pp. 615-618
    • Harshman, R.B.1    Yamazaki, H.2
  • 47
    • 0028032946 scopus 로고
    • Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB)
    • Heath, R.J., Jackowski, S., and Rock, C.O. (1994) Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB). J Biol Chem 269: 26584-26590.
    • (1994) J Biol Chem , vol.269 , pp. 26584-26590
    • Heath, R.J.1    Jackowski, S.2    Rock, C.O.3
  • 48
    • 0027258590 scopus 로고
    • Characterization of RNA and DNA synthesis in Escherichia coli strains devoid of ppGpp
    • Hernandez, V.J., and Bremer, H. (1993) Characterization of RNA and DNA synthesis in Escherichia coli strains devoid of ppGpp. J Biol Chem 268: 10851-10862.
    • (1993) J Biol Chem , vol.268 , pp. 10851-10862
    • Hernandez, V.J.1    Bremer, H.2
  • 49
    • 0017795562 scopus 로고
    • Hypoxanthine phosphoribosyltransferase and guanine phosphoribosyltransferase from enteric bacteria
    • Hochstadt, J. (1978) Hypoxanthine phosphoribosyltransferase and guanine phosphoribosyltransferase from enteric bacteria. Methods Enzymol 51: 549-558.
    • (1978) Methods Enzymol , vol.51 , pp. 549-558
    • Hochstadt, J.1
  • 50
    • 0015502060 scopus 로고
    • The regulation of purine utilization in bacteria. V. Inhibition of purine phosphoribosyltransferase activities and purine uptake in isolated membrane vesicles by guanosine tetraphosphate
    • Hochstadt-Ozer, J., and Cashel, M. (1972) The regulation of purine utilization in bacteria. V. Inhibition of purine phosphoribosyltransferase activities and purine uptake in isolated membrane vesicles by guanosine tetraphosphate. J Biol Chem 247: 7067-7072.
    • (1972) J Biol Chem , vol.247 , pp. 7067-7072
    • Hochstadt-Ozer, J.1    Cashel, M.2
  • 51
    • 0015218643 scopus 로고
    • The regulation of purine utilization in bacteria. I. Purification of adenine phosphoribosyltransferase from Escherichia coli K12 and control of activity by nucleotides
    • Hochstadt-Ozer, J., and Stadtman, E.R. (1971) The regulation of purine utilization in bacteria. I. Purification of adenine phosphoribosyltransferase from Escherichia coli K12 and control of activity by nucleotides. J Biol Chem 246: 5294-5303.
    • (1971) J Biol Chem , vol.246 , pp. 5294-5303
    • Hochstadt-Ozer, J.1    Stadtman, E.R.2
  • 52
    • 1842766260 scopus 로고    scopus 로고
    • Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]
    • Hogg, T., Mechold, U., Malke, H., Cashel, M., and Hilgenfeld, R. (2004) Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]. Cell 117: 57-68.
    • (2004) Cell , vol.117 , pp. 57-68
    • Hogg, T.1    Mechold, U.2    Malke, H.3    Cashel, M.4    Hilgenfeld, R.5
  • 53
    • 0033215301 scopus 로고    scopus 로고
    • Structure-function studies of adenylosuccinate synthetase from Escherichia coli
    • Honzatko, R.B., and Fromm, H.J. (1999) Structure-function studies of adenylosuccinate synthetase from Escherichia coli. Arch Biochem Biophys 370: 1-8.
    • (1999) Arch Biochem Biophys , vol.370 , pp. 1-8
    • Honzatko, R.B.1    Fromm, H.J.2
  • 54
    • 0033581009 scopus 로고    scopus 로고
    • Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase
    • Hou, Z., Cashel, M., Fromm, H.J., and Honzatko, R.B. (1999) Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase. J Biol Chem 274: 17505-17510.
    • (1999) J Biol Chem , vol.274 , pp. 17505-17510
    • Hou, Z.1    Cashel, M.2    Fromm, H.J.3    Honzatko, R.B.4
  • 55
    • 80055008762 scopus 로고    scopus 로고
    • The enzymatic activities of the Escherichia coli basic aliphatic amino acid decarboxylases exhibit a pH zone of inhibition
    • Kanjee, U., Gutsche, I., Ramachandran, S., and Houry, W. (2011a) The enzymatic activities of the Escherichia coli basic aliphatic amino acid decarboxylases exhibit a pH zone of inhibition. Biochemistry 50: 9388-9398.
    • (2011) Biochemistry , vol.50 , pp. 9388-9398
    • Kanjee, U.1    Gutsche, I.2    Ramachandran, S.3    Houry, W.4
  • 56
    • 79952280501 scopus 로고    scopus 로고
    • Linking the bacterial acid stress and stringent responses - the structure of the inducible lysine decarboxylase
    • Kanjee, U., Gutsche, I., Alexopoulos, E., Zhao, B., Thibault, G., Liu, K., etal. (2011b) Linking the bacterial acid stress and stringent responses - the structure of the inducible lysine decarboxylase. EMBO J 30: 931-944.
    • (2011) EMBO J , vol.30 , pp. 931-944
    • Kanjee, U.1    Gutsche, I.2    Alexopoulos, E.3    Zhao, B.4    Thibault, G.5    Liu, K.6
  • 57
    • 0030585061 scopus 로고    scopus 로고
    • The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange
    • al-Karadaghi, S., Aevarsson, A., Garber, M., Zheltonosova, J., and Liljas, A. (1996) The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure 4: 555-565.
    • (1996) Structure , vol.4 , pp. 555-565
    • al-Karadaghi, S.1    Aevarsson, A.2    Garber, M.3    Zheltonosova, J.4    Liljas, A.5
  • 58
    • 33749646813 scopus 로고    scopus 로고
    • Physiological analysis of the stringent response elicited in an extreme thermophilic bacterium, Thermus thermophilus
    • Kasai, K., Nishizawa, T., Takahashi, K., Hosaka, T., Aoki, H., and Ochi, K. (2006) Physiological analysis of the stringent response elicited in an extreme thermophilic bacterium, Thermus thermophilus. J Bacteriol 188: 7111-7122.
    • (2006) J Bacteriol , vol.188 , pp. 7111-7122
    • Kasai, K.1    Nishizawa, T.2    Takahashi, K.3    Hosaka, T.4    Aoki, H.5    Ochi, K.6
  • 59
    • 0034737468 scopus 로고    scopus 로고
    • Structure of the RNA polymerase domain of E.coli primase
    • Keck, J.L., Roche, D.D., Lynch, A.S., and Berger, J.M. (2000) Structure of the RNA polymerase domain of E.coli primase. Science 287: 2482-2486.
    • (2000) Science , vol.287 , pp. 2482-2486
    • Keck, J.L.1    Roche, D.D.2    Lynch, A.S.3    Berger, J.M.4
  • 60
    • 0344826574 scopus 로고    scopus 로고
    • Characterization of the hipA7 allele of Escherichia coli and evidence that high persistence is governed by (p)ppGpp synthesis
    • Korch, S.B., Henderson, T.A., and Hill, T.M. (2003) Characterization of the hipA7 allele of Escherichia coli and evidence that high persistence is governed by (p)ppGpp synthesis. Mol Microbiol 50: 1199-1213.
    • (2003) Mol Microbiol , vol.50 , pp. 1199-1213
    • Korch, S.B.1    Henderson, T.A.2    Hill, T.M.3
  • 61
    • 37549035447 scopus 로고    scopus 로고
    • Structure of the PPX/GPPA phosphatase from Aquifex aeolicus in complex with the alarmone ppGpp
    • Kristensen, O., Ross, B., and Gajhede, M. (2008) Structure of the PPX/GPPA phosphatase from Aquifex aeolicus in complex with the alarmone ppGpp. J Mol Biol 375: 1469-1476.
    • (2008) J Mol Biol , vol.375 , pp. 1469-1476
    • Kristensen, O.1    Ross, B.2    Gajhede, M.3
  • 62
    • 0030771435 scopus 로고    scopus 로고
    • Guanosine tetra- and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli
    • Kuroda, A., Murphy, H., Cashel, M., and Kornberg, A. (1997) Guanosine tetra- and pentaphosphate promote accumulation of inorganic polyphosphate in Escherichia coli. J Biol Chem 272: 21240-21243.
    • (1997) J Biol Chem , vol.272 , pp. 21240-21243
    • Kuroda, A.1    Murphy, H.2    Cashel, M.3    Kornberg, A.4
  • 63
    • 0033955874 scopus 로고    scopus 로고
    • Emergency derepression: stringency allows RNA polymerase to override negative control by an active repressor
    • Kvint, K., Hosbond, C., Farewell, A., Nybroe, O., and Nystrom, T. (2000) Emergency derepression: stringency allows RNA polymerase to override negative control by an active repressor. Mol Microbiol 35: 435-443.
    • (2000) Mol Microbiol , vol.35 , pp. 435-443
    • Kvint, K.1    Hosbond, C.2    Farewell, A.3    Nybroe, O.4    Nystrom, T.5
  • 64
    • 66449110287 scopus 로고    scopus 로고
    • DOCK 6: combining techniques to model RNA-small molecule complexes
    • Lang, P.T., Brozell, S.R., Mukherjee, S., Pettersen, E.F., Meng, E.C., Thomas, V., etal. (2009) DOCK 6: combining techniques to model RNA-small molecule complexes. RNA 15: 1219-1230.
    • (2009) RNA , vol.15 , pp. 1219-1230
    • Lang, P.T.1    Brozell, S.R.2    Mukherjee, S.3    Pettersen, E.F.4    Meng, E.C.5    Thomas, V.6
  • 65
    • 47249083116 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MazG, the regulator of nutritional stress response
    • Lee, S., Kim, M.H., Kang, B.S., Kim, J.S., Kim, G.H., Kim, Y.G., and Kim, K.J. (2008) Crystal structure of Escherichia coli MazG, the regulator of nutritional stress response. J Biol Chem 283: 15232-15240.
    • (2008) J Biol Chem , vol.283 , pp. 15232-15240
    • Lee, S.1    Kim, M.H.2    Kang, B.S.3    Kim, J.S.4    Kim, G.H.5    Kim, Y.G.6    Kim, K.J.7
  • 66
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site
    • Leesong, M., Henderson, B.S., Gillig, J.R., Schwab, J.M., and Smith, J.L. (1996) Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4: 253-264.
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 67
    • 14444275280 scopus 로고
    • Inhibition of in vitro protein synthesis by ppGpp
    • Legault, L., Jeantet, C., and Gros, F. (1972) Inhibition of in vitro protein synthesis by ppGpp. FEBS Lett 27: 71-75.
    • (1972) FEBS Lett , vol.27 , pp. 71-75
    • Legault, L.1    Jeantet, C.2    Gros, F.3
  • 68
    • 0042570711 scopus 로고    scopus 로고
    • Purification and characterization of YihA, an essential GTP-binding protein from Escherichia coli
    • Lehoux, I.E., Mazzulla, M.J., Baker, A., and Petit, C.M. (2003) Purification and characterization of YihA, an essential GTP-binding protein from Escherichia coli. Protein Expr Purif 30: 203-209.
    • (2003) Protein Expr Purif , vol.30 , pp. 203-209
    • Lehoux, I.E.1    Mazzulla, M.J.2    Baker, A.3    Petit, C.M.4
  • 69
    • 79955047348 scopus 로고    scopus 로고
    • Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA
    • Lemke, J.J., Sanchez-Vazquez, P., Burgos, H.L., Hedberg, G., Ross, W., and Gourse, R.L. (2011) Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA. Proc Natl Acad Sci USA 108: 5712-5717.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5712-5717
    • Lemke, J.J.1    Sanchez-Vazquez, P.2    Burgos, H.L.3    Hedberg, G.4    Ross, W.5    Gourse, R.L.6
  • 70
    • 0021112246 scopus 로고
    • Purification and characterization of Escherichia coli guanine-xanthine phosphoribosyltransferase produced by a high efficiency expression plasmid utilizing a lambda PL promoter and CI857 temperature-sensitive repressor
    • Liu, S.W., and Milman, G. (1983) Purification and characterization of Escherichia coli guanine-xanthine phosphoribosyltransferase produced by a high efficiency expression plasmid utilizing a lambda PL promoter and CI857 temperature-sensitive repressor. J Biol Chem 258: 7469-7475.
    • (1983) J Biol Chem , vol.258 , pp. 7469-7475
    • Liu, S.W.1    Milman, G.2
  • 71
    • 0345869701 scopus 로고    scopus 로고
    • The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition
    • Lohkamp, B., McDermott, G., Campbell, S.A., Coggins, J.R., and Lapthorn, A.J. (2004) The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition. J Mol Biol 336: 131-144.
    • (2004) J Mol Biol , vol.336 , pp. 131-144
    • Lohkamp, B.1    McDermott, G.2    Campbell, S.A.3    Coggins, J.R.4    Lapthorn, A.J.5
  • 72
    • 0016808133 scopus 로고
    • The involvement of guanosine 5-diphosphate-3-diphosphate in the regulation of phospholipid biosynthesis in Escherichia coli. Lack of ppGpp inhibition of acyltransfer from acyl-ACP to sn-glycerol 3-phosphate
    • Lueking, D.R., and Goldfine, H. (1975) The involvement of guanosine 5-diphosphate-3-diphosphate in the regulation of phospholipid biosynthesis in Escherichia coli. Lack of ppGpp inhibition of acyltransfer from acyl-ACP to sn-glycerol 3-phosphate. J Biol Chem 250: 4911-4917.
    • (1975) J Biol Chem , vol.250 , pp. 4911-4917
    • Lueking, D.R.1    Goldfine, H.2
  • 74
    • 18044367581 scopus 로고    scopus 로고
    • ppGpp: a global regulator in Escherichia coli
    • Magnusson, L.U., Farewell, A., and Nystrom, T. (2005) ppGpp: a global regulator in Escherichia coli. Trends Microbiol 13: 236-242.
    • (2005) Trends Microbiol , vol.13 , pp. 236-242
    • Magnusson, L.U.1    Farewell, A.2    Nystrom, T.3
  • 75
    • 34447540221 scopus 로고    scopus 로고
    • Identical, independent, and opposing roles of ppGpp and DksA in Escherichia coli
    • Magnusson, L.U., Gummesson, B., Joksimovic, P., Farewell, A., and Nystrom, T. (2007) Identical, independent, and opposing roles of ppGpp and DksA in Escherichia coli. J Bacteriol 189: 5193-5202.
    • (2007) J Bacteriol , vol.189 , pp. 5193-5202
    • Magnusson, L.U.1    Gummesson, B.2    Joksimovic, P.3    Farewell, A.4    Nystrom, T.5
  • 76
    • 33846887420 scopus 로고    scopus 로고
    • Phylogenetic distribution of translational GTPases in bacteria
    • Margus, T., Remm, M., and Tenson, T. (2007) Phylogenetic distribution of translational GTPases in bacteria. BMC Genomics 8: 15.
    • (2007) BMC Genomics , vol.8 , pp. 15
    • Margus, T.1    Remm, M.2    Tenson, T.3
  • 77
    • 79952664822 scopus 로고    scopus 로고
    • Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation
    • Martinelli, L.K., Ducati, R.G., Rosado, L.A., Breda, A., Selbach, B.P., Santos, D.S., and Basso, L.A. (2011) Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation. Mol Biosyst 7: 1289-1305.
    • (2011) Mol Biosyst , vol.7 , pp. 1289-1305
    • Martinelli, L.K.1    Ducati, R.G.2    Rosado, L.A.3    Breda, A.4    Selbach, B.P.5    Santos, D.S.6    Basso, L.A.7
  • 78
    • 0037082125 scopus 로고    scopus 로고
    • Degradation of L-glutamate dehydrogenase from Escherichia coli: allosteric regulation of enzyme stability
    • Maurizi, M.R., and Rasulova, F. (2002) Degradation of L-glutamate dehydrogenase from Escherichia coli: allosteric regulation of enzyme stability. Arch Biochem Biophys 397: 206-216.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 206-216
    • Maurizi, M.R.1    Rasulova, F.2
  • 79
    • 0015803248 scopus 로고
    • Regulation of phospholipid synthesis in Escherichia coli by guanosine tetraphosphate
    • Merlie, J.P., and Pizer, L.I. (1973) Regulation of phospholipid synthesis in Escherichia coli by guanosine tetraphosphate. J Bacteriol 116: 355-366.
    • (1973) J Bacteriol , vol.116 , pp. 355-366
    • Merlie, J.P.1    Pizer, L.I.2
  • 80
    • 0024327693 scopus 로고
    • Protein sequences encoded by the relA and the spoT genes of Escherichia coli are interrelated
    • Metzger, S., Sarubbi, E., Glaser, G., and Cashel, M. (1989) Protein sequences encoded by the relA and the spoT genes of Escherichia coli are interrelated. J Biol Chem 264: 9122-9125.
    • (1989) J Biol Chem , vol.264 , pp. 9122-9125
    • Metzger, S.1    Sarubbi, E.2    Glaser, G.3    Cashel, M.4
  • 81
    • 0015577309 scopus 로고
    • The interaction of guanosine 5′-diphosphate, 2′ (3′)-diphosphate with the bacterial elongation factor Tu
    • Miller, D.L., Cashel, M., and Weissbach, H. (1973) The interaction of guanosine 5′-diphosphate, 2′ (3′)-diphosphate with the bacterial elongation factor Tu. Arch Biochem Biophys 154: 675-682.
    • (1973) Arch Biochem Biophys , vol.154 , pp. 675-682
    • Miller, D.L.1    Cashel, M.2    Weissbach, H.3
  • 82
    • 33749021074 scopus 로고    scopus 로고
    • The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor
    • Milon, P., Tischenko, E., Tomsic, J., Caserta, E., Folkers, G., La Teana, A., etal. (2006) The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor. Proc Natl Acad Sci USA 103: 13962-13967.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13962-13967
    • Milon, P.1    Tischenko, E.2    Tomsic, J.3    Caserta, E.4    Folkers, G.5    La Teana, A.6
  • 83
    • 0017577475 scopus 로고
    • Synergistic inhibition of ATP phosphoribosyltransferase by guanosine tetraphosphate and histidine
    • Morton, D.P., and Parsons, S.M. (1977) Synergistic inhibition of ATP phosphoribosyltransferase by guanosine tetraphosphate and histidine. Biochem Biophys Res Commun 74: 172-177.
    • (1977) Biochem Biophys Res Commun , vol.74 , pp. 172-177
    • Morton, D.P.1    Parsons, S.M.2
  • 84
    • 33745221184 scopus 로고    scopus 로고
    • ppGpp with DksA controls gene expression in the locus of enterocyte effacement (LEE) pathogenicity island of enterohaemorrhagic Escherichia coli through activation of two virulence regulatory genes
    • Nakanishi, N., Abe, H., Ogura, Y., Hayashi, T., Tashiro, K., Kuhara, S., etal. (2006) ppGpp with DksA controls gene expression in the locus of enterocyte effacement (LEE) pathogenicity island of enterohaemorrhagic Escherichia coli through activation of two virulence regulatory genes. Mol Microbiol 61: 194-205.
    • (2006) Mol Microbiol , vol.61 , pp. 194-205
    • Nakanishi, N.1    Abe, H.2    Ogura, Y.3    Hayashi, T.4    Tashiro, K.5    Kuhara, S.6
  • 85
    • 8544232750 scopus 로고    scopus 로고
    • Growth versus maintenance: a trade-off dictated by RNA polymerase availability and sigma factor competition?
    • Nystrom, T. (2004) Growth versus maintenance: a trade-off dictated by RNA polymerase availability and sigma factor competition? Mol Microbiol 54: 855-862.
    • (2004) Mol Microbiol , vol.54 , pp. 855-862
    • Nystrom, T.1
  • 86
    • 0020321919 scopus 로고
    • Evidence that Bacillus subtilis sporulation induced by the stringent response is caused by the decrease in GTP or GDP
    • Ochi, K., Kandala, J., and Freese, E. (1982) Evidence that Bacillus subtilis sporulation induced by the stringent response is caused by the decrease in GTP or GDP. J Bacteriol 151: 1062-1065.
    • (1982) J Bacteriol , vol.151 , pp. 1062-1065
    • Ochi, K.1    Kandala, J.2    Freese, E.3
  • 87
    • 0019792355 scopus 로고
    • Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes
    • Pao, C.C., and Dyess, B.T. (1981) Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes. Biochim Biophys Acta 677: 358-362.
    • (1981) Biochim Biophys Acta , vol.677 , pp. 358-362
    • Pao, C.C.1    Dyess, B.T.2
  • 88
    • 20344363655 scopus 로고    scopus 로고
    • DksA potentiates direct activation of amino acid promoters by ppGpp
    • Paul, B.J., Berkmen, M.B., and Gourse, R.L. (2005) DksA potentiates direct activation of amino acid promoters by ppGpp. Proc Natl Acad Sci USA 102: 7823-7828.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7823-7828
    • Paul, B.J.1    Berkmen, M.B.2    Gourse, R.L.3
  • 89
    • 67650465604 scopus 로고    scopus 로고
    • The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli
    • Persky, N.S., Ferullo, D.J., Cooper, D.L., Moore, H.R., and Lovett, S.T. (2009) The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli. Mol Microbiol 73: 253-266.
    • (2009) Mol Microbiol , vol.73 , pp. 253-266
    • Persky, N.S.1    Ferullo, D.J.2    Cooper, D.L.3    Moore, H.R.4    Lovett, S.T.5
  • 90
    • 0021100471 scopus 로고
    • The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes
    • Pingoud, A., Gast, F.U., Block, W., and Peters, F. (1983) The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes. J Biol Chem 258: 14200-14205.
    • (1983) J Biol Chem , vol.258 , pp. 14200-14205
    • Pingoud, A.1    Gast, F.U.2    Block, W.3    Peters, F.4
  • 91
    • 0015735116 scopus 로고
    • Stringent control of fatty acid synthesis in Escherichia coli. Possible regulation of acetyl coenzyme A carboxylase by ppGpp
    • Polakis, S.E., Guchhait, R.B., and Lane, M.D. (1973) Stringent control of fatty acid synthesis in Escherichia coli. Possible regulation of acetyl coenzyme A carboxylase by ppGpp. J Biol Chem 248: 7957-7966.
    • (1973) J Biol Chem , vol.248 , pp. 7957-7966
    • Polakis, S.E.1    Guchhait, R.B.2    Lane, M.D.3
  • 93
    • 79551662182 scopus 로고    scopus 로고
    • ppGpp is the major source of growth rate control in E.coli
    • Potrykus, K., Murphy, H., Philippe, N., and Cashel, M. (2011) ppGpp is the major source of growth rate control in E.coli. Environ Microbiol 13: 563-575.
    • (2011) Environ Microbiol , vol.13 , pp. 563-575
    • Potrykus, K.1    Murphy, H.2    Philippe, N.3    Cashel, M.4
  • 94
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • Powers, T., and Walter, P. (1995) Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269: 1422-1424.
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 95
    • 33745170717 scopus 로고    scopus 로고
    • The structure of the exopolyphosphatase (PPX) from Escherichia coli O157:H7 suggests a binding mode for long polyphosphate chains
    • Rangarajan, E.S., Nadeau, G., Li, Y., Wagner, J., Hung, M.N., Schrag, J.D., etal. (2006) The structure of the exopolyphosphatase (PPX) from Escherichia coli O157:H7 suggests a binding mode for long polyphosphate chains. J Mol Biol 359: 1249-1260.
    • (2006) J Mol Biol , vol.359 , pp. 1249-1260
    • Rangarajan, E.S.1    Nadeau, G.2    Li, Y.3    Wagner, J.4    Hung, M.N.5    Schrag, J.D.6
  • 96
    • 0022621213 scopus 로고
    • Purification and some properties of uracil phosphoribosyltransferase from Escherichia coli K12
    • Rasmussen, U.B., Mygind, B., and Nygaard, P. (1986) Purification and some properties of uracil phosphoribosyltransferase from Escherichia coli K12. Biochim Biophys Acta 881: 268-275.
    • (1986) Biochim Biophys Acta , vol.881 , pp. 268-275
    • Rasmussen, U.B.1    Mygind, B.2    Nygaard, P.3
  • 97
    • 0027159053 scopus 로고
    • Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily
    • Reizer, J., Reizer, A., Saier, M.H., Jr, Bork, P., and Sander, C. (1993) Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily. Trends Biochem Sci 18: 247-248.
    • (1993) Trends Biochem Sci , vol.18 , pp. 247-248
    • Reizer, J.1    Reizer, A.2    Saier Jr., M.H.3    Bork, P.4    Sander, C.5
  • 98
    • 0029121141 scopus 로고
    • Direct correlation between overproduction of guanosine 3′,5′-bispyrophosphate (ppGpp) and penicillin tolerance in Escherichia coli
    • Rodionov, D.G., and Ishiguro, E.E. (1995) Direct correlation between overproduction of guanosine 3′, 5′-bispyrophosphate (ppGpp) and penicillin tolerance in Escherichia coli. J Bacteriol 177: 4224-4229.
    • (1995) J Bacteriol , vol.177 , pp. 4224-4229
    • Rodionov, D.G.1    Ishiguro, E.E.2
  • 99
    • 0021231777 scopus 로고
    • ppGpp inhibition of elongation factors Tu, G and Ts during polypeptide synthesis
    • Rojas, A.M., Ehrenberg, M., Andersson, S.G., and Kurland, C.G. (1984) ppGpp inhibition of elongation factors Tu, G and Ts during polypeptide synthesis. Mol Gen Genet 197: 36-45.
    • (1984) Mol Gen Genet , vol.197 , pp. 36-45
    • Rojas, A.M.1    Ehrenberg, M.2    Andersson, S.G.3    Kurland, C.G.4
  • 100
    • 0024670025 scopus 로고
    • Genetic regulation of glycogen biosynthesis in Escherichia coli: in vitro effects of cyclic AMP and guanosine 5′-diphosphate 3′-diphosphate and analysis of in vivo transcripts
    • Romeo, T., and Preiss, J. (1989) Genetic regulation of glycogen biosynthesis in Escherichia coli: in vitro effects of cyclic AMP and guanosine 5′-diphosphate 3′-diphosphate and analysis of in vivo transcripts. J Bacteriol 171: 2773-2782.
    • (1989) J Bacteriol , vol.171 , pp. 2773-2782
    • Romeo, T.1    Preiss, J.2
  • 101
    • 0027171032 scopus 로고
    • Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties
    • Romeo, T., Gong, M., Liu, M.Y., and Brun-Zinkernagel, A.M. (1993) Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties. J Bacteriol 175: 4744-4755.
    • (1993) J Bacteriol , vol.175 , pp. 4744-4755
    • Romeo, T.1    Gong, M.2    Liu, M.Y.3    Brun-Zinkernagel, A.M.4
  • 103
    • 0028960079 scopus 로고
    • ppGpp-mediated regulation of DNA replication and cell division in Escherichia coli
    • Schreiber, G., Ron, E.Z., and Glaser, G. (1995) ppGpp-mediated regulation of DNA replication and cell division in Escherichia coli. Curr Microbiol 30: 27-32.
    • (1995) Curr Microbiol , vol.30 , pp. 27-32
    • Schreiber, G.1    Ron, E.Z.2    Glaser, G.3
  • 104
    • 33745520400 scopus 로고    scopus 로고
    • Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element
    • Scrima, A., and Wittinghofer, A. (2006) Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element. EMBO J 25: 2940-2951.
    • (2006) EMBO J , vol.25 , pp. 2940-2951
    • Scrima, A.1    Wittinghofer, A.2
  • 105
    • 0022367020 scopus 로고
    • Purification and properties of orotate phosphoribosyltransferases from Escherichia coli K-12, and its derivative purine-sensitive mutant
    • Shimosaka, M., Fukuda, Y., Murata, K., and Kimura, A. (1985) Purification and properties of orotate phosphoribosyltransferases from Escherichia coli K-12, and its derivative purine-sensitive mutant. J Biochem 98: 1689-1697.
    • (1985) J Biochem , vol.98 , pp. 1689-1697
    • Shimosaka, M.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 106
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution
    • Song, H., Parsons, M.R., Rowsell, S., Leonard, G., and Phillips, S.E. (1999) Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. J Mol Biol 285: 1245-1256.
    • (1999) J Mol Biol , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.5
  • 107
    • 0031936775 scopus 로고    scopus 로고
    • The relation between ppGpp and the PHO regulon in Escherichia coli
    • Spira, B., and Yagil, E. (1998) The relation between ppGpp and the PHO regulon in Escherichia coli. Mol Gen Genet 257: 469-477.
    • (1998) Mol Gen Genet , vol.257 , pp. 469-477
    • Spira, B.1    Yagil, E.2
  • 108
    • 0029079412 scopus 로고
    • Guanosine 3′,5′-bispyrophosphate (ppGpp) synthesis in cells of Escherichia coli starved for Pi
    • Spira, B., Silberstein, N., and Yagil, E. (1995) Guanosine 3′, 5′-bispyrophosphate (ppGpp) synthesis in cells of Escherichia coli starved for Pi. J Bacteriol 177: 4053-4058.
    • (1995) J Bacteriol , vol.177 , pp. 4053-4058
    • Spira, B.1    Silberstein, N.2    Yagil, E.3
  • 109
    • 0018421738 scopus 로고
    • Guanosine 5′-diphosphate-3′-diphosphate inhibition of adenylosuccinate synthetase
    • Stayton, M.M., and Fromm, H.J. (1979) Guanosine 5′-diphosphate-3′-diphosphate inhibition of adenylosuccinate synthetase. J Biol Chem 254: 2579-2581.
    • (1979) J Biol Chem , vol.254 , pp. 2579-2581
    • Stayton, M.M.1    Fromm, H.J.2
  • 110
    • 0017059482 scopus 로고
    • Inhibition of E.coli beta-hydroxydecanoyl thioester dehydrase by ppGpp
    • Stein, J.P., Jr, and Bloch, K.E. (1976) Inhibition of E.coli beta-hydroxydecanoyl thioester dehydrase by ppGpp. Biochem Biophys Res Commun 73: 881-884.
    • (1976) Biochem Biophys Res Commun , vol.73 , pp. 881-884
    • Stein Jr., J.P.1    Bloch, K.E.2
  • 111
    • 0000975897 scopus 로고
    • A genetic locus for the regulation of ribonucleic acid synthesis
    • Stent, G.S., and Brenner, S. (1961) A genetic locus for the regulation of ribonucleic acid synthesis. Proc Natl Acad Sci USA 47: 2005-2014.
    • (1961) Proc Natl Acad Sci USA , vol.47 , pp. 2005-2014
    • Stent, G.S.1    Brenner, S.2
  • 112
    • 0027410057 scopus 로고
    • Guanosine tetraphosphate inhibits protein synthesis in vivo. A possible protective mechanism for starvation stress in Escherichia coli
    • Svitil, A.L., Cashel, M., and Zyskind, J.W. (1993) Guanosine tetraphosphate inhibits protein synthesis in vivo. A possible protective mechanism for starvation stress in Escherichia coli. J Biol Chem 268: 2307-2311.
    • (1993) J Biol Chem , vol.268 , pp. 2307-2311
    • Svitil, A.L.1    Cashel, M.2    Zyskind, J.W.3
  • 113
    • 0035542686 scopus 로고    scopus 로고
    • Comparison of DeltarelA strains of Escherichia coli and Salmonella enterica serovar Typhimurium suggests a role for ppGpp in attenuation regulation of branched-chain amino acid biosynthesis
    • Tedin, K., and Norel, F. (2001) Comparison of DeltarelA strains of Escherichia coli and Salmonella enterica serovar Typhimurium suggests a role for ppGpp in attenuation regulation of branched-chain amino acid biosynthesis. J Bacteriol 183: 6184-6196.
    • (2001) J Bacteriol , vol.183 , pp. 6184-6196
    • Tedin, K.1    Norel, F.2
  • 114
    • 0039765528 scopus 로고    scopus 로고
    • Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA
    • Thanbichler, M., Bock, A., and Goody, R.S. (2000) Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA. J Biol Chem 275: 20458-20466.
    • (2000) J Biol Chem , vol.275 , pp. 20458-20466
    • Thanbichler, M.1    Bock, A.2    Goody, R.S.3
  • 115
    • 22544464455 scopus 로고    scopus 로고
    • RNA polymerase modulators and DNA repair activities resolve conflicts between DNA replication and transcription
    • Trautinger, B.W., Jaktaji, R.P., Rusakova, E., and Lloyd, R.G. (2005) RNA polymerase modulators and DNA repair activities resolve conflicts between DNA replication and transcription. Mol Cell 19: 247-258.
    • (2005) Mol Cell , vol.19 , pp. 247-258
    • Trautinger, B.W.1    Jaktaji, R.P.2    Rusakova, E.3    Lloyd, R.G.4
  • 116
    • 33144488588 scopus 로고    scopus 로고
    • Guanosine 3′,5′-bispyrophosphate coordinates global gene expression during glucose-lactose diauxie in Escherichia coli
    • Traxler, M.F., Chang, D.E., and Conway, T. (2006) Guanosine 3′, 5′-bispyrophosphate coordinates global gene expression during glucose-lactose diauxie in Escherichia coli. Proc Natl Acad Sci USA 103: 2374-2379.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2374-2379
    • Traxler, M.F.1    Chang, D.E.2    Conway, T.3
  • 118
    • 79551663315 scopus 로고    scopus 로고
    • Discretely calibrated regulatory loops controlled by ppGpp partition gene induction across the 'feast to famine' gradient in Escherichia coli
    • Traxler, M.F., Zacharia, V.M., Marquardt, S., Summers, S.M., Nguyen, H.T., Stark, S.E., and Conway, T. (2011) Discretely calibrated regulatory loops controlled by ppGpp partition gene induction across the 'feast to famine' gradient in Escherichia coli. Mol Microbiol 79: 830-845.
    • (2011) Mol Microbiol , vol.79 , pp. 830-845
    • Traxler, M.F.1    Zacharia, V.M.2    Marquardt, S.3    Summers, S.M.4    Nguyen, H.T.5    Stark, S.E.6    Conway, T.7
  • 119
    • 78651319979 scopus 로고    scopus 로고
    • Ongoing and future developments at the Universal Protein Resource
    • UniProt Consortium
    • UniProt Consortium (2011) Ongoing and future developments at the Universal Protein Resource. Nucleic Acids Res 39: D214-D219.
    • (2011) Nucleic Acids Res , vol.39
  • 120
    • 18444368425 scopus 로고    scopus 로고
    • Iron limitation induces SpoT-dependent accumulation of ppGpp in Escherichia coli
    • Vinella, D., Albrecht, C., Cashel, M., and D'Ari, R. (2005) Iron limitation induces SpoT-dependent accumulation of ppGpp in Escherichia coli. Mol Microbiol 56: 958-970.
    • (2005) Mol Microbiol , vol.56 , pp. 958-970
    • Vinella, D.1    Albrecht, C.2    Cashel, M.3    D'Ari, R.4
  • 121
    • 0032475913 scopus 로고    scopus 로고
    • Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase
    • Vos, S., Parry, R.J., Burns, M.R., de Jersey, J., and Martin, J.L. (1998) Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase. J Mol Biol 282: 875-889.
    • (1998) J Mol Biol , vol.282 , pp. 875-889
    • Vos, S.1    Parry, R.J.2    Burns, M.R.3    de Jersey, J.4    Martin, J.L.5
  • 122
    • 40049090539 scopus 로고    scopus 로고
    • Still looking for the magic spot: the crystallographically defined binding site for ppGpp on RNA polymerase is unlikely to be responsible for rRNA transcription regulation
    • Vrentas, C.E., Gaal, T., Berkmen, M.B., Rutherford, S.T., Haugen, S., Vassylyev, D.G., etal. (2008) Still looking for the magic spot: the crystallographically defined binding site for ppGpp on RNA polymerase is unlikely to be responsible for rRNA transcription regulation. J Mol Biol 377: 551-564.
    • (2008) J Mol Biol , vol.377 , pp. 551-564
    • Vrentas, C.E.1    Gaal, T.2    Berkmen, M.B.3    Rutherford, S.T.4    Haugen, S.5    Vassylyev, D.G.6
  • 123
    • 33847383586 scopus 로고    scopus 로고
    • Nutritional control of elongation of DNA replication by (p)ppGpp
    • Wang, J.D., Sanders, G.M., and Grossman, A.D. (2007) Nutritional control of elongation of DNA replication by (p)ppGpp. Cell 128: 865-875.
    • (2007) Cell , vol.128 , pp. 865-875
    • Wang, J.D.1    Sanders, G.M.2    Grossman, A.D.3
  • 125
    • 0032830481 scopus 로고    scopus 로고
    • Evolution of aminoacyl-tRNA synthetases - analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events
    • Wolf, Y.I., Aravind, L., Grishin, N.V., and Koonin, E.V. (1999) Evolution of aminoacyl-tRNA synthetases - analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res 9: 689-710.
    • (1999) Genome Res , vol.9 , pp. 689-710
    • Wolf, Y.I.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 126
    • 3843074167 scopus 로고    scopus 로고
    • The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase
    • Wout, P., Pu, K., Sullivan, S.M., Reese, V., Zhou, S., Lin, B., and Maddock, J.R. (2004) The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase. J Bacteriol 186: 5249-5257.
    • (2004) J Bacteriol , vol.186 , pp. 5249-5257
    • Wout, P.1    Pu, K.2    Sullivan, S.M.3    Reese, V.4    Zhou, S.5    Lin, B.6    Maddock, J.R.7
  • 127
    • 0025992789 scopus 로고
    • Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations
    • Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G., and Cashel, M. (1991) Residual guanosine 3′, 5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J Biol Chem 266: 5980-5990.
    • (1991) J Biol Chem , vol.266 , pp. 5980-5990
    • Xiao, H.1    Kalman, M.2    Ikehara, K.3    Zemel, S.4    Glaser, G.5    Cashel, M.6
  • 128
    • 0141504234 scopus 로고    scopus 로고
    • Temperature-sensitive growth and decreased thermotolerance associated with relA mutations in Escherichia coli
    • Yang, X., and Ishiguro, E.E. (2003) Temperature-sensitive growth and decreased thermotolerance associated with relA mutations in Escherichia coli. J Bacteriol 185: 5765-5771.
    • (2003) J Bacteriol , vol.185 , pp. 5765-5771
    • Yang, X.1    Ishiguro, E.E.2
  • 129
    • 33748781176 scopus 로고    scopus 로고
    • Feedback control of ribosome synthesis in Escherichia coli is dependent on eight critical amino acids
    • Zhang, X., Liang, S.T., and Bremer, H. (2006) Feedback control of ribosome synthesis in Escherichia coli is dependent on eight critical amino acids. Biochimie 88: 1145-1155.
    • (2006) Biochimie , vol.88 , pp. 1145-1155
    • Zhang, X.1    Liang, S.T.2    Bremer, H.3


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