메뉴 건너뛰기




Volumn 190, Issue 9, 2008, Pages 3236-3243

RelA functionally suppresses the growth defect caused by a mutation in the G domain of the essential Der protein

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN; PROTEIN DER; SYNTHETASE; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG;

EID: 42549155787     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01758-07     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 33751075737 scopus 로고    scopus 로고
    • A cooperative and critical role for both G-domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA
    • Bharat, A., M. Jiang, S. M. Sullivan, J. R. Maddock, and E. D. Brown. 2006. A cooperative and critical role 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
  • 2
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1990. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 8:125-132.
    • (1990) Nature , vol.8 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 3
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature 10:117-127.
    • (1991) Nature , vol.10 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 5
    • 0036849768 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Obg GTP binding protein
    • Buglino, J., V. Shen, P. Hakimian, and C. D. Lima. 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
  • 6
    • 0034596029 scopus 로고    scopus 로고
    • The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23S ribosomal RNA methyltransferase
    • Caldas, T., E. Binet, P. Bouloc, A. Costa, J. Desgres, and G. Richarme. 2000. The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23S ribosomal RNA methyltransferase. J. Biol. Chem. 22:16414-16419.
    • (2000) J. Biol. Chem , vol.22 , pp. 16414-16419
    • Caldas, T.1    Binet, E.2    Bouloc, P.3    Costa, A.4    Desgres, J.5    Richarme, G.6
  • 7
    • 42549172381 scopus 로고    scopus 로고
    • Cashel, M., D. Gentry, V. J. Hernandez, and D. Vinella. 1996. The stringent response, p. 1488-1496. In F. C. Neidhardt, R. Curtis, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., 1. ASM Press, Washington, DC.
    • Cashel, M., D. Gentry, V. J. Hernandez, and D. Vinella. 1996. The stringent response, p. 1488-1496. In F. C. Neidhardt, R. Curtis, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1. ASM Press, Washington, DC.
  • 8
    • 0031949801 scopus 로고    scopus 로고
    • The mediator for stringent control, ppGpp, binds to the beta-subunit of Escherichia coli RNA polymerase
    • Chatterji, D., N. Fujita, and A. Ishihama. 1998. The mediator for stringent control, ppGpp, binds to the beta-subunit of Escherichia coli RNA polymerase. Genes Cells 3:279-287.
    • (1998) Genes Cells , vol.3 , pp. 279-287
    • Chatterji, D.1    Fujita, N.2    Ishihama, A.3
  • 9
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 12
    • 0035253621 scopus 로고    scopus 로고
    • KH domain: One motif, two folds
    • Grishin, N. V. 2001. KH domain: one motif, two folds. Nucleic Acids Res. 29:638-643.
    • (2001) Nucleic Acids Res , vol.29 , pp. 638-643
    • Grishin, N.V.1
  • 13
    • 0035150018 scopus 로고    scopus 로고
    • Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain
    • Gropp, M., Y. Strausz, M. Gross, and G. Glaser. 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
    • 0013830963 scopus 로고
    • Mode of action of the herbicide, 3-amino-1,2,4-triazole(amitrole): Inhibition of an enzyme of histidine biosynthesis
    • Hilton, J. L., P. C. Kearney, and B. N. Ames. 1965. Mode of action of the herbicide, 3-amino-1,2,4-triazole(amitrole): inhibition of an enzyme of histidine biosynthesis. Arch. Biochem. Biophys. 112:544-547.
    • (1965) Arch. Biochem. Biophys , vol.112 , pp. 544-547
    • Hilton, J.L.1    Kearney, P.C.2    Ames, B.N.3
  • 15
    • 0035903205 scopus 로고    scopus 로고
    • An essential GTPase, der, containing double GTP-binding domains from Escherichia coli and Thermotoga maritima
    • Hwang, J., and M. Inouye. 2001. An essential GTPase, der, containing double GTP-binding domains from Escherichia coli and Thermotoga maritima. J. Biol. Chem. 276:31415-31421.
    • (2001) J. Biol. Chem , vol.276 , pp. 31415-31421
    • Hwang, J.1    Inouye, M.2
  • 16
    • 33748486487 scopus 로고    scopus 로고
    • The tandem GTPase, Dcr, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli
    • Hwang, J., and M. Inouye. 2006. The tandem GTPase, Dcr, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli. Mol. Microbiol. 61:1660-1672.
    • (2006) Mol. Microbiol , vol.61 , pp. 1660-1672
    • Hwang, J.1    Inouye, M.2
  • 18
    • 0035788799 scopus 로고    scopus 로고
    • Deficiency of essential GTP-binding protein ObgE in Escherichia coli inhibits chromosome partition
    • Kobayashi, G., S. Moriya, and C. Wada. 2001. Deficiency of essential GTP-binding protein ObgE in Escherichia coli inhibits chromosome partition. Mol. Microbiol. 41:1037-1051.
    • (2001) Mol. Microbiol , vol.41 , pp. 1037-1051
    • Kobayashi, G.1    Moriya, S.2    Wada, C.3
  • 19
    • 18044367581 scopus 로고    scopus 로고
    • ppGpp: A global regulator in Escherichia coli
    • Magnussen, L. U., A. Farewell, and T. Nystrom. 2005. ppGpp: a global regulator in Escherichia coli. Trends Microbiol. 13:236-242.
    • (2005) Trends Microbiol , vol.13 , pp. 236-242
    • Magnussen, L.U.1    Farewell, A.2    Nystrom, T.3
  • 20
    • 0033968143 scopus 로고    scopus 로고
    • A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation
    • Mehr, I. J., C. D. Long, C. D. Serkin, and H. S. Seifert. 2000. A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation. Genetics 154:523-532.
    • (2000) Genetics , vol.154 , pp. 523-532
    • Mehr, I.J.1    Long, C.D.2    Serkin, C.D.3    Seifert, H.S.4
  • 22
    • 0036855348 scopus 로고    scopus 로고
    • Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis
    • Morimoto, T., P. C. Loh, T. Hirai, K. Asai, K. Kobayashi, S. Moriya, and N. Ogasawara. 2002. Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis. Microbiology 148:3539-3552.
    • (2002) Microbiology , vol.148 , pp. 3539-3552
    • Morimoto, T.1    Loh, P.C.2    Hirai, T.3    Asai, K.4    Kobayashi, K.5    Moriya, S.6    Ogasawara, N.7
  • 23
    • 33747584905 scopus 로고    scopus 로고
    • The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding
    • Muench, S. P., L. Xu, S. E. Sedelnikova, and D. W. Rice. 2006. The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding. Proc. Natl. Acad. Sci. USA 103:12359-12364.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12359-12364
    • Muench, S.P.1    Xu, L.2    Sedelnikova, S.E.3    Rice, D.W.4
  • 24
    • 34248328786 scopus 로고    scopus 로고
    • Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae
    • Raskin, D. M., N. Judson, and J. J. Mekalanos. 2007. Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae. Proc. Natl. Acad. Sci. USA 104:4636-4641.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4636-4641
    • Raskin, D.M.1    Judson, N.2    Mekalanos, J.J.3
  • 25
    • 1842848075 scopus 로고    scopus 로고
    • Domain arrangement of Der, a switch protein containing two GTPase domains
    • Robinson, V. L., J. Hwang, E. Fox, M. Inouye, and A. M. Stock. 2002. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure 10:1649-1658.
    • (2002) Structure , vol.10 , pp. 1649-1658
    • Robinson, V.L.1    Hwang, J.2    Fox, E.3    Inouye, M.4    Stock, A.M.5
  • 26
    • 0014004365 scopus 로고
    • Polysomes extracted from Escherichia coli by freeze-thaw-lysozyme lysis
    • Ron, E. Z., R. E. Kohler, and B. D. Davis. 1966. Polysomes extracted from Escherichia coli by freeze-thaw-lysozyme lysis. Science 153:1119-1120.
    • (1966) Science , vol.153 , pp. 1119-1120
    • Ron, E.Z.1    Kohler, R.E.2    Davis, B.D.3
  • 27
    • 0020316476 scopus 로고
    • Temperature dependence of RNA synthesis parameters in Escherichia coli
    • Ryals, J., R. Little, and H. Bremer. 1982. Temperature dependence of RNA synthesis parameters in Escherichia coli. J. Bacteriol. 151:879-887.
    • (1982) J. Bacteriol , vol.151 , pp. 879-887
    • Ryals, J.1    Little, R.2    Bremer, H.3
  • 30
    • 0016825910 scopus 로고
    • Guanosine 5′-diphosphate 3′-diphosphate (ppGpp): Positive effector for histidine operon transcription and general signal for amino-acid deficiency
    • Stephens, J. C., S. W. Artz, and B. N. Ames. 1975. Guanosine 5′-diphosphate 3′-diphosphate (ppGpp): positive effector for histidine operon transcription and general signal for amino-acid deficiency. Proc. Natl. Acad. Sci. USA 72:4389-4393.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4389-4393
    • Stephens, J.C.1    Artz, S.W.2    Ames, B.N.3
  • 31
    • 0019474551 scopus 로고
    • X-ray determination of the GDP-binding site of Escherichia coli elongation factor Tu by substitution with ppGpp
    • Suck, D., and W. Kabsch. 1981. X-ray determination of the GDP-binding site of Escherichia coli elongation factor Tu by substitution with ppGpp. FEBS Lett. 126:120-122.
    • (1981) FEBS Lett , vol.126 , pp. 120-122
    • Suck, D.1    Kabsch, W.2
  • 32
    • 0036237999 scopus 로고    scopus 로고
    • Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase
    • Tan, J., U. Jakob, and J. C. Bardwell. 2002. Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. J. Bacteriol. 184:2692-2698.
    • (2002) J. Bacteriol , vol.184 , pp. 2692-2698
    • Tan, J.1    Jakob, U.2    Bardwell, J.C.3
  • 33
    • 0035847007 scopus 로고    scopus 로고
    • Binding of the transcription effector ppGpp to Escherichia coli RNA polymerase is allosteric, modular, and occurs near the N terminus of the beta′-subunit
    • Toulokhonov, I. I., I. Shulgina, and V. J. Hernandez. 2001. Binding of the transcription effector ppGpp to Escherichia coli RNA polymerase is allosteric, modular, and occurs near the N terminus of the beta′-subunit. J. Biol. Chem. 276:1220-1225.
    • (2001) J. Biol. Chem , vol.276 , pp. 1220-1225
    • Toulokhonov, I.I.1    Shulgina, I.2    Hernandez, V.J.3
  • 34
    • 0022476632 scopus 로고
    • The oncogenic activation of human p21ras by a novel mechanism
    • Walter, M., S. G. Clark, and A. D. Levinson. 1986. The oncogenic activation of human p21ras by a novel mechanism. Science 233:649-652.
    • (1986) Science , vol.233 , pp. 649-652
    • Walter, M.1    Clark, S.G.2    Levinson, A.D.3
  • 35
    • 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., K. Pu, S. M. Sullivan, V. Reese, S. Zhou, B. Lin, and J. R. Maddock. 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
  • 36
    • 0025992789 scopus 로고
    • Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations
    • Xiao, H., M. Kaiman, K. Ikehara, S. Zemel, G. Glaser, and M. Cashel. 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    Kaiman, M.2    Ikehara, K.3    Zemel, S.4    Glaser, G.5    Cashel, M.6
  • 37
    • 0034751687 scopus 로고    scopus 로고
    • Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli
    • Yang, X., and E. E. Ishiguro. 2001. Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli. J. Bacteriol. 183:6532-6537.
    • (2001) J. Bacteriol , vol.183 , pp. 6532-6537
    • Yang, X.1    Ishiguro, E.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.