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Volumn 15, Issue 6, 2006, Pages 1449-1464

Molecular dissection of the mycobacterial stringent response protein Rel

Author keywords

Multimerization; ppGpp; Rel domains; Rel protein; Stringent response

Indexed keywords

TRANSCRIPTION FACTOR REL; TRANSFER RNA;

EID: 33744481783     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062117006     Document Type: Article
Times cited : (74)

References (49)
  • 1
    • 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
  • 2
    • 0032791894 scopus 로고    scopus 로고
    • Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis
    • Avarbock, D., Salem, J., Li, L.S., Wang, Z.M., and Rubin, H. 1999. Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene 233: 261-269.
    • (1999) Gene , vol.233 , pp. 261-269
    • Avarbock, D.1    Salem, J.2    Li, L.S.3    Wang, Z.M.4    Rubin, H.5
  • 5
    • 0028142648 scopus 로고
    • Domain organization of RNA polymerase a subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding
    • Blatter, E.E., Ross, W., Tang, H., Gourse, R.L., and Ebright, R.H. 1994. Domain organization of RNA polymerase a subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding. Cell 78: 889-896.
    • (1994) Cell , vol.78 , pp. 889-896
    • Blatter, E.E.1    Ross, W.2    Tang, H.3    Gourse, R.L.4    Ebright, R.H.5
  • 7
    • 0035075387 scopus 로고    scopus 로고
    • Revisiting the stringent response, ppGpp and starvation signaling
    • Chatterji, D. and Ojha, A.K. 2001. Revisiting the stringent response, ppGpp and starvation signaling. Curr. Opin. Microbiol. 4: 160-165.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 160-165
    • Chatterji, D.1    Ojha, A.K.2
  • 9
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L.A. and Johnson Jr., W.C. 1986. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155: 155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 12
    • 0034461403 scopus 로고    scopus 로고
    • Control of asgE expression during growth and development of Myxococcus xanthus
    • Garza, A.G., Harris, B.Z., Greenberg, B.M., and Singer, M. 2000. Control of asgE expression during growth and development of Myxococcus xanthus. J. Bacteriol. 182: 6622-6629.
    • (2000) J. Bacteriol. , vol.182 , pp. 6622-6629
    • Garza, A.G.1    Harris, B.Z.2    Greenberg, B.M.3    Singer, M.4
  • 13
    • 0035150018 scopus 로고    scopus 로고
    • Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain
    • Gropp, M., Strausz, Y., Gross, M., and Glaser, G. 2001. Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain. J. Bacteriol. 183: 570-579.
    • (2001) J. Bacteriol. , vol.183 , pp. 570-579
    • Gropp, M.1    Strausz, Y.2    Gross, M.3    Glaser, G.4
  • 14
    • 0007825206 scopus 로고
    • Synthesis of guanosine tetra- and pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes
    • Haseltine, W.A. and Block, R. 1973. Synthesis of guanosine tetra- and pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes. Proc. Natl. Acad. Sci. 70: 1564-1568.
    • (1973) Proc. Natl. Acad. Sci. , vol.70 , pp. 1564-1568
    • Haseltine, W.A.1    Block, R.2
  • 15
    • 0025772728 scopus 로고
    • Functional specialization within the a-subunit of Escherichia coli RNA polymerase
    • Hayward, R.S., Igarashi, K., and Ishihama, A. 1991. Functional specialization within the a-subunit of Escherichia coli RNA polymerase. J. Mol. Biol. 221: 23-29.
    • (1991) J. Mol. Biol. , vol.221 , pp. 23-29
    • Hayward, R.S.1    Igarashi, K.2    Ishihama, A.3
  • 16
    • 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
    • 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. 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
  • 17
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF-A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. and Thornton, J.M. 1996. PROMOTIF-A program to identify and analyze structural motifs in proteins. Protein Sci. 5: 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 18
    • 0025778597 scopus 로고
    • Bipartite functional map of the E. coli RNA polymerase α subunit: Involvement of the C-terminal region in transcription activation by cAMP-CRP
    • Igarashi, K. and Ishihama, A. 1991. Bipartite functional map of the E. coli RNA polymerase α subunit: Involvement of the C-terminal region in transcription activation by cAMP-CRP. Cell 65: 1015-1022.
    • (1991) Cell , vol.65 , pp. 1015-1022
    • Igarashi, K.1    Ishihama, A.2
  • 19
    • 19544365903 scopus 로고    scopus 로고
    • Identification and characterization of rel promoter element of Mycobacterium tuberculosis
    • Jain, V., Sujatha, S., Ojha, A.K., and Chatterji, D. 2005. Identification and characterization of rel promoter element of Mycobacterium tuberculosis. Gene 351: 149-157.
    • (2005) Gene , vol.351 , pp. 149-157
    • Jain, V.1    Sujatha, S.2    Ojha, A.K.3    Chatterji, D.4
  • 21
    • 0342872087 scopus 로고    scopus 로고
    • Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein
    • Kim, D.W., Gwack, Y., Han, J.H., and Choe, J. 1997. Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein. Virus Res. 49: 17-25.
    • (1997) Virus Res. , vol.49 , pp. 17-25
    • Kim, D.W.1    Gwack, Y.2    Han, J.H.3    Choe, J.4
  • 22
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami, S., Akiyama, Y., and Ito, K. 1995. Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett. 364: 55-58.
    • (1995) FEBS Lett. , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 23
    • 0028860275 scopus 로고
    • A procedure for the rapid preparation of guanosine tetraphosphate (ppGpp) from Escherichia coli ribosomes
    • Krohn, M. and Wagner, R. 1995. A procedure for the rapid preparation of guanosine tetraphosphate (ppGpp) from Escherichia coli ribosomes. Anal. Biochem. 225: 188-190.
    • (1995) Anal. Biochem. , vol.225 , pp. 188-190
    • Krohn, M.1    Wagner, R.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0036837744 scopus 로고    scopus 로고
    • Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation
    • Lee, P.A., Buchanan, G., Stanley, N.R., Berks, B.C., and Palmer, T. 2002. Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation. J. Bacteriol. 184: 5871-5879.
    • (2002) J. Bacteriol. , vol.184 , pp. 5871-5879
    • Lee, P.A.1    Buchanan, G.2    Stanley, N.R.3    Berks, B.C.4    Palmer, T.5
  • 26
    • 15244344475 scopus 로고    scopus 로고
    • Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism
    • Liberles, J.S., Thorolfsson, M., and Martinez, A. 2005. Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism. Amino Acids 28: 1-12.
    • (2005) Amino Acids , vol.28 , pp. 1-12
    • Liberles, J.S.1    Thorolfsson, M.2    Martinez, A.3
  • 29
    • 0031829736 scopus 로고    scopus 로고
    • The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp-synthesizing and -degrading activities
    • Martinez-Costa, O.H., Fernandez-Moreno, M.A., and Malpartida, F. 1998. The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp-synthesizing and -degrading activities. J. Bacteriol. 180: 4123-4132.
    • (1998) J. Bacteriol. , vol.180 , pp. 4123-4132
    • Martinez-Costa, O.H.1    Fernandez-Moreno, M.A.2    Malpartida, F.3
  • 30
    • 4444320817 scopus 로고    scopus 로고
    • Deletion of the rel gene in Mycobacterium smegmatis reduces its stationary phase survival without altering the cell-surface associated properties
    • Mathew, R., Ojha, A.K., Karande, A., and Chatterji, D. 2004. Deletion of the rel gene in Mycobacterium smegmatis reduces its stationary phase survival without altering the cell-surface associated properties. Curr. Sci. 86: 149-153.
    • (2004) Curr. Sci. , vol.86 , pp. 149-153
    • Mathew, R.1    Ojha, A.K.2    Karande, A.3    Chatterji, D.4
  • 31
    • 0029924014 scopus 로고    scopus 로고
    • Functional analysis of a relA/spoT gene homolog from Streptococcus equisimilis
    • Mechold, U., Cashel, M., Steiner, K., Gentry, D., and Malke, H. 1996. Functional analysis of a relA/spoT gene homolog from Streptococcus equisimilis. J. Bacteriol. 178: 1401-1411.
    • (1996) J. Bacteriol. , vol.178 , pp. 1401-1411
    • Mechold, U.1    Cashel, M.2    Steiner, K.3    Gentry, D.4    Malke, H.5
  • 33
    • 0016159839 scopus 로고
    • Studies on the effect of starvation on mycobacteria
    • Nyka, W. 1974. Studies on the effect of starvation on mycobacteria. Infect. Immun. 9: 843-850.
    • (1974) Infect. Immun. , vol.9 , pp. 843-850
    • Nyka, W.1
  • 34
    • 0033917102 scopus 로고    scopus 로고
    • High intracellular level of guanosine tetraphosphate in Mycobacterium smegmatis changes the morphology of the bacterium
    • Ojha, A.K., Mukherjee, T.K., and Chatterji, D. 2000. High intracellular level of guanosine tetraphosphate in Mycobacterium smegmatis changes the morphology of the bacterium. Infect. Immun. 68: 4084-4091.
    • (2000) Infect. Immun. , vol.68 , pp. 4084-4091
    • Ojha, A.K.1    Mukherjee, T.K.2    Chatterji, D.3
  • 36
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D.N., Pappin, D.J., Creasy, D.M., and Cottrell, J.S. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 37
    • 0033872759 scopus 로고    scopus 로고
    • The stringent response of Mycobacterium tuberculosis is required for long-term survival
    • Primm, T.P., Andersen, S.J., Mizrahi, V., Avarbock, D., Rubin, H., and Barry III, C.E. 2000. The stringent response of Mycobacterium tuberculosis is required for long-term survival. J. Bacteriol. 182: 4889-4898.
    • (2000) J. Bacteriol. , vol.182 , pp. 4889-4898
    • Primm, T.P.1    Andersen, S.J.2    Mizrahi, V.3    Avarbock, D.4    Rubin, H.5    Barry III, C.E.6
  • 38
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S.W. and Glockner, J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20: 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 39
    • 0033617335 scopus 로고    scopus 로고
    • The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
    • Sankaranarayanan, R., Dock-Bregeon, A.C., Romby, P., Caillet, J., Springer, M., Rees, B., Ehresmann, C., Ehresmann, B., and Moras, D. 1999. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97: 371-381.
    • (1999) Cell , vol.97 , pp. 371-381
    • Sankaranarayanan, R.1    Dock-Bregeon, A.C.2    Romby, P.3    Caillet, J.4    Springer, M.5    Rees, B.6    Ehresmann, C.7    Ehresmann, B.8    Moras, D.9
  • 40
    • 0028951187 scopus 로고
    • The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase
    • Schuller, D.J., Grant, G.A., and Banaszak, L.J. 1995. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 2: 69-76.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 69-76
    • Schuller, D.J.1    Grant, G.A.2    Banaszak, L.J.3
  • 41
    • 0038167027 scopus 로고    scopus 로고
    • Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA
    • Shenoy, A.R. and Visweswariah, S.S. 2003. Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA. Anal. Biochem. 319: 335-336.
    • (2003) Anal. Biochem. , vol.319 , pp. 335-336
    • Shenoy, A.R.1    Visweswariah, S.S.2
  • 42
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R.W. 2000. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287: 252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 44
    • 0035036356 scopus 로고    scopus 로고
    • Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2)
    • Sun, J., Hesketh, A., and Bibb, M. 2001. Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2). J. Bacteriol. 183: 3488-3498.
    • (2001) J. Bacteriol. , vol.183 , pp. 3488-3498
    • Sun, J.1    Hesketh, A.2    Bibb, M.3
  • 45
    • 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
  • 46
    • 0025204703 scopus 로고
    • Estimation of protein secondary structure and error analysis from circular dichroism spectra
    • van Stokkum, I.H., Spoelder, H.J., Bloemendal, M., van Grondelle, R., and Groen, F.C. 1990. Estimation of protein secondary structure and error analysis from circular dichroism spectra. Anal. Biochem. 191: 110-118.
    • (1990) Anal. Biochem. , vol.191 , pp. 110-118
    • Van Stokkum, I.H.1    Spoelder, H.J.2    Bloemendal, M.3    Van Grondelle, R.4    Groen, F.C.5
  • 47
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of non-replicating persistence
    • Wayne, L.G. and Hayes, L.G. 1996. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of non-replicating persistence. Infect. Immun. 64: 2062-2069.
    • (1996) Infect. Immun. , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 48
    • 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
  • 49
    • 1442281182 scopus 로고    scopus 로고
    • Minimal machinery of RNA polymerase holoenzyme sufficient for promoter melting
    • Young, B.A., Gruber, T.M., and Gross, C.A. 2004. Minimal machinery of RNA polymerase holoenzyme sufficient for promoter melting. Science 303: 1382-1384.
    • (2004) Science , vol.303 , pp. 1382-1384
    • Young, B.A.1    Gruber, T.M.2    Gross, C.A.3


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