참고문헌
- Aravind, L. and E.V. Koonin. 1998. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem Sci. 23, 469-472 https://doi.org/10.1016/S0968-0004(98)01293-6
- Artsimovitch, I., V. Patlan, S. Sekine, M.N. Vassylyeva, T. Hosaka, K. Ochi, S. Yokoyama and D.G. Vassylyev. 2004. Structural basis for transcription regulation by alarmone ppGpp. Cell 117, 299-310 https://doi.org/10.1016/S0092-8674(04)00401-5
-
Avarbock, A., D. Avarbock, J.S. Teh, M. Buckstein, Z.M. Wang and H. Rubin. 2005. Functional regulation of the opposing (p)ppGpp synthetase/hydrolase activities of
$Rel_{Mtb}$ from Mycobacterium tuberculosis. Biochemistry 44, 9913-9923 https://doi.org/10.1021/bi0505316 -
Avarbock, D., A. Avarbock and H. Rubin. 2000. Differential regulation of opposing
$Rel_{Mtb}$ activities by the aminoacylation state of a tRNA.ribosome.mRNA.$Rel_{Mtb}$ complex. Biochemistry 39, 11640-11648 https://doi.org/10.1021/bi001256k - Avarbock, D., J. Salem, L.S. Li, Z.M. Wang and H. Rubin. 1999. Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene 233, 261-269 https://doi.org/10.1016/S0378-1119(99)00114-6
- Bashyam, M.D., D. Kaushal, S.K. Dasgupta and A.K. Tyagi. 1996. A study of mycobacterial transcriptional apparatus: identification of novel features in promoter elements. J. Bacteriol. 178, 4847-4853 https://doi.org/10.1128/jb.178.16.4847-4853.1996
- Baysse, C., M. Cullinane, V. Denervaud, E. Burrowes, J.M. Dow, J.P. Morrissey, L. Tam, J.T. Trevors and F. O'Gara. 2005. Modulation of quorum sensing in Pseudomonas aeruginosa through alteration of membrane properties. Microbiology 151, 2529-2542 https://doi.org/10.1099/mic.0.28185-0
- Calderon-Flores, A., G. Du Pont, A. Huerta-Saquero, H. Merchant-Larios, L. Servin-Gonzalez and S. Duran. 2005. The stringent response is required for amino acid and nitrate utilization, nod factor regulation, nodulation, and nitrogen fixation in Rhizobium etli. J. Bacteriol. 187, 5075-5083 https://doi.org/10.1128/JB.187.15.5075-5083.2005
- Cashel, M. 1974. Preparation of guanosine tetraphosphate (ppGpp) and guanosine pentaphosphate (pppGpp) from Escherichia coli ribosomes. Anal. Biochem. 57, 100-107 https://doi.org/10.1016/0003-2697(74)90056-6
- Cashel, M. 1975. Regulation of bacterial ppGpp and pppGpp. Annu. Rev. Microbiol. 29, 301-318 https://doi.org/10.1146/annurev.mi.29.100175.001505
- Cashel, M., D.R. Gentry, V.J. Hernandez and D. Vinella. 1996. The stringent response, p.1458-1496. In F.C. Neidhardt, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter and H.E. Umbarger (eds.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. 2nd ed. ASM Press, Washington, D.C
- Cellini, A., G.L. Scoarughi, P. Poggiali, I. Santino, R. Sessa, P. Donini and C. Cimmino. 2004. Stringent control in the archaeal genus Sulfolobus. Res. Microbiol. 155, 98-104 https://doi.org/10.1016/j.resmic.2003.11.006
- Chakraburtty, R. and M. Bibb. 1997. The ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation. J. Bacteriol. 179, 5854-5861 https://doi.org/10.1128/jb.179.18.5854-5861.1997
- 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 https://doi.org/10.1046/j.1365-2443.1998.00190.x
- Chatterji, D. and A.K. Ojha. 2001. Revisiting the stringent response, ppGpp and starvation signaling. Curr. Opin. Microbiol. 4, 160-165 https://doi.org/10.1016/S1369-5274(00)00182-X
- Crawford, E.W., Jr. and L.J. Shimkets. 2000. The stringent response in Myxococcus xanthus is regulated by SocE and the CsgA C-signaling protein. Genes Dev. 14, 483-492
- Dahl, J.L., K. Arora, H.I. Boshoff, D.C. Whiteford, S.A. Pacheco, O.J. Walsh, D. Lau-Bonilla, W.B. Davis and A.G. Garza. 2005. The relA homolog of Mycobacterium smegmatis affects cell appearance, viability, and gene expression. J. Bacteriol. 187, 2439-2447 https://doi.org/10.1128/JB.187.7.2439-2447.2005
-
Dahl, J.L., C.N. Kraus, H.I. Boshoff, B. Doan, K. Foley, D. Avarbock, G. Kaplan, V. Mizrahi, H. Rubin and C.E. Barry, 3rd. 2003. The role of
$Rel_{Mtb}$ -mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Proc. Natl. Acad. Sci. USA 100, 10026-10031 - Erickson, D.L., J.L. Lines, E.C. Pesci, V. Venturi and D.G. Storey. 2004. Pseudomonas aeruginosa relA contributes to virulence in Drosophila melanogaster. Infect. Immun. 72, 5638-5645 https://doi.org/10.1128/IAI.72.10.5638-5645.2004
- Fisher, S.D., A.D. Reger, A. Baum and S.A. Hill. 2005. RelA alone appears essential for (p)ppGpp production when Neisseria gonorrhoeae encounters nutritional stress. FEMS Microbiol. Lett. 248, 1-8 https://doi.org/10.1016/j.femsle.2005.05.014
- Garza, A.G., B.Z. Harris, B.M. Greenberg and M. Singer. 2000. Control of asgE expression during growth and development of Myxococcus xanthus. J. Bacteriol. 182, 6622-6629 https://doi.org/10.1128/JB.182.23.6622-6629.2000
- Gaynor, E.C., D.H. Wells, J.K. MacKichan and S. Falkow. 2005. The Campylobacter jejuni stringent response controls specific stress survival and virulence-associated phenotypes. Mol. Microbiol. 56, 8-27 https://doi.org/10.1111/j.1365-2958.2005.04525.x
- Gentry, D., H. Xiao, R. Burgess and M. Cashel. 1991. The omega subunit of Escherichia coli K-12 RNA polymerase is not required for stringent RNA control in vivo. J. Bacteriol. 173, 3901-3903 https://doi.org/10.1128/jb.173.12.3901-3903.1991
- Gentry, D.R. and R.R. Burgess. 1989. rpoZ, encoding the omega subunit of Escherichia coli RNA polymerase, is in the same operon as spoT. J. Bacteriol. 171, 1271-1277 https://doi.org/10.1128/jb.171.3.1271-1277.1989
- 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 https://doi.org/10.1128/JB.183.2.570-579.2001
- Gupta, S., S.B. Pandit, N. Srinivasan and D. Chatterji. 2002. Proteomics analysis of carbon-starved Mycobacterium smegmatis: induction of Dps-like protein. Protein Eng. 15, 503-512 https://doi.org/10.1093/protein/15.6.503
- Hammer, B.K. and M.S. Swanson. 1999. Co-ordination of Legionella pneumophila virulence with entry into stationary phase by ppGpp. Mol. Microbiol. 33, 721-731 https://doi.org/10.1046/j.1365-2958.1999.01519.x
- Haralalka, S., S. Nandi and R.K. Bhadra. 2003. Mutation in the relA gene of Vibrio cholerae affects in vitro and in vivo expression of virulence factors. J. Bacteriol. 185, 4672-4682 https://doi.org/10.1128/JB.185.16.4672-4682.2003
- Harris, B.Z., D. Kaiser and M. Singer. 1998. The guanosine nucleotide (p)ppGpp initiates development and A-factor production in Myxococcus xanthus. Genes Dev. 12, 1022-1035 https://doi.org/10.1101/gad.12.7.1022
- Haseltine, W.A. and R. Block. 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. USA 70, 1564-1568
- Hogg, T., U. Mechold, H. Malke, M. Cashel and R. Hilgenfeld. 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 https://doi.org/10.1016/S0092-8674(04)00260-0
- Hoyt, S. and G.H. Jones. 1999. relA is required for actinomycin production in Streptomyces antibioticus. J. Bacteriol. 181, 3824-3829
- Igarashi, K., N. Fujita and A. Ishihama. 1989. Promoter selectivity of Escherichia coli RNA polymerase: omega factor is responsible for the ppGpp sensitivity. Nucleic Acids Res. 17, 8755-8765 https://doi.org/10.1093/nar/17.21.8755
- Inaoka, T., K. Takahashi, M. Ohnishi-Kameyama, M. Yoshida and K. Ochi. 2003. Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-operatively regulate the production of an antibiotic bacilysin in Bacillus subtilis. J. Biol. Chem. 278, 2169-2176 https://doi.org/10.1074/jbc.M208722200
- Jain, V., S. Sujatha, A.K. Ojha and D. Chatterji. 2005. Identification and characterization of rel promoter element of Mycobacterium tuberculosis. Gene 351, 149-157 https://doi.org/10.1016/j.gene.2005.03.038
- Jin, W., H.K. Kim, J.Y. Kim, S.G. Kang, S.H. Lee and K.J. Lee. 2004. Cephamycin C production is regulated by relA and rsh genes in Streptomyces clavuligerus ATCC27064. J. Biotechnol. 114, 81-87 https://doi.org/10.1016/j.jbiotec.2004.06.010
- Jishage, M., K. Kvint, V. Shingler and T. Nystrom. 2002. Regulation of sigma factor competition by the alarmone ppGpp. Genes Dev. 16, 1260-1270 https://doi.org/10.1101/gad.227902
- Johnson, G.S., C.R. Adler, J.J. Collins and D. Court. 1979. Role of the spoT gene product and manganese ion in the metabolism of guanosine 5'-diphosphate 3'-diphosphate in Escherichia coli. J. Biol. Chem. 254, 5483-5487
- Kvint, K., A. Farewell and T. Nystrom. 2000. RpoS-dependent promoters require guanosine tetraphosphate for induction even in the presence of high levels of sigma(s). J. Biol. Chem. 275, 14795-14798 https://doi.org/10.1074/jbc.C000128200
- Manabe, Y.C. and W.R. Bishai. 2000. Latent Mycobacterium tuberculosis-persistence, patience, and winning by waiting. Nat. Med. 6, 1327-1329 https://doi.org/10.1038/82139
- Martinez-Costa, O.H., M.A. Fernandez-Moreno and F. Malpartida. 1998. The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp-synthesizing and -degrading activities. J. Bacteriol. 180, 4123-4132
- Mathew, R., A.K. Ojha, A. Karande and D. Chatterji. 2004. Deletion of the rel gene in Mycobacterium smegmatis reduces its staionary phase survival without altering the cell-surface associated properties. Curr. Sci. 86, 149-153
- Mayuri, G. Bagchi, T.K. Das and J.S. Tyagi. 2002. Molecular analysis of the dormancy response in Mycobacterium smegmatis: expression analysis of genes encoding the DevR-DevS two-component system, Rv3134c and chaperone alpha-crystallin homologues. FEMS Microbiol. Lett. 211, 231-237
- Mechold, U., M. Cashel, K. Steiner, D. Gentry and H. Malke. 1996. Functional analysis of a relA/spoT gene homolog from Streptococcus equisimilis. J. Bacteriol. 178, 1401-1411 https://doi.org/10.1128/jb.178.5.1401-1411.1996
- Mechold, U., H. Murphy, L. Brown and M. Cashel. 2002. Intramolecular regulation of the opposing (p)ppGpp catalytic activities of Rel(Seq), the Rel/Spo enzyme from Streptococcus equisimilis. J. Bacteriol. 184, 2878-2888 https://doi.org/10.1128/JB.184.11.2878-2888.2002
- Mittenhuber, G. 2001. Comparative genomics and evolution of genes encoding bacterial (p)ppGpp synthetases/hydrolases (the Rel, RelA and SpoT proteins). J. Mol. Microbiol. Biotechnol. 3, 585-600
- Moris, M., K. Braeken, E. Schoeters, C. Verreth, S. Beullens, J. Vanderleyden and J. Michiels. 2005. Effective symbiosis between Rhizobium etli and Phaseolus vulgaris requires the alarmone ppGpp. J. Bacteriol. 187, 5460-5469 https://doi.org/10.1128/JB.187.15.5460-5469.2005
- Mukherjee, R., M. Gomez, N. Jayaraman, I. Smith and D. Chatterji. 2005. Hyperglycosylation of glycopeptidolipid of Mycobacterium smegmatis under nutrient starvation: structural studies. Microbiology 151, 2385-2392 https://doi.org/10.1099/mic.0.27908-0
- Mulder, M.A., H. Zappe and L.M. Steyn. 1997. Mycobacterial promoters. Tuber. Lung Dis. 78, 211-223 https://doi.org/10.1016/S0962-8479(97)90001-0
- Ojha, A.K., T.K. Mukherjee and D. Chatterji. 2000. High intracellular level of guanosine tetraphosphate in Mycobacterium smegmatis changes the morphology of the bacterium. Infect. Immun. 68, 4084-4091 https://doi.org/10.1128/IAI.68.7.4084-4091.2000
- Parrish, N.M., J.D. Dick and W.R. Bishai. 1998. Mechanisms of latency in Mycobacterium tuberculosis. Trends. Microbiol. 6, 107-112 https://doi.org/10.1016/S0966-842X(98)01216-5
- Paul, B.J., M.M. Barker, W. Ross, D.A. Schneider, C. Webb, J.W. Foster and R.L. Gourse. 2004. DksA: a critical component of the transcription initiation machinery that potentiates the regulation of rRNA promoters by ppGpp and the initiating NTP. Cell 118, 311-322 https://doi.org/10.1016/j.cell.2004.07.009
- Paul, B.J., M.B. Berkmen and R.L. Gourse. 2005. DksA potentiates direct activation of amino acid promoters by ppGpp. Proc. Natl. Acad. Sci. USA 102, 7823-7828
- Perederina, A., V. Svetlov, M.N. Vassylyeva, T.H. Tahirov, S. Yokoyama, I. Artsimovitch and D.G. Vassylyev. 2004. Regulation through the secondary channel-structural framework for ppGpp-DksA synergism during transcription. Cell 118, 297-309 https://doi.org/10.1016/j.cell.2004.06.030
- Pizarro-Cerda, J. and K. Tedin. 2004. The bacterial signal molecule, ppGpp, regulates Salmonella virulence gene expression. Mol. Microbiol. 52, 1827-1844 https://doi.org/10.1111/j.1365-2958.2004.04122.x
- Primm, T.P., S.J. Andersen, V. Mizrahi, D. Avarbock, H. Rubin and C.E. Barry, 3rd. 2000. The stringent response of Mycobacterium tuberculosis is required for long-term survival. J. Bacteriol. 182, 4889-4898 https://doi.org/10.1128/JB.182.17.4889-4898.2000
- Reddy, P.S., A. Raghavan and D. Chatterji. 1995. Evidence for a ppGpp-binding site on Escherichia coli RNA polymerase: proximity relationship with the rifampicin-binding domain. Mol. Microbiol. 15, 255-265 https://doi.org/10.1111/j.1365-2958.1995.tb02240.x
- Reyrat, J.M. and D. Kahn. 2001. Mycobacterium smegmatis: an absurd model for tuberculosis? Trends. Microbiol. 9, 472-474
- Scoarughi, G.L., C. Cimmino and P. Donini. 1999. Helicobacter pylori: a eubacterium lacking the stringent response. J. Bacteriol. 181, 552-555
- Song, M., H.J. Kim, E.Y. Kim, M. Shin, H.C. Lee, Y. Hong, J.H. Rhee, H. Yoon, S. Ryu, S. Lim and H.E. Choy. 2004. ppGpp-dependent stationary phase induction of genes on Salmonella pathogenicity island 1. J. Biol. Chem. 279, 34183-34190 https://doi.org/10.1074/jbc.M313491200
- Sun, J., A. Hesketh and M. Bibb. 2001. Functional analysis of relA and rshA, two relA/spoT homologues of Streptomyces coelicolor A3(2). J. Bacteriol. 183, 3488-3498 https://doi.org/10.1128/JB.183.11.3488-3498.2001
- Svitil, A.L., M. Cashel and J.W. Zyskind. 1993. Guanosine tetraphosphate inhibits protein synthesis in vivo. A possible protective mechanism for starvation stress in Escherichia coli. J. Biol. Chem. 268, 2307-2311
- Takahashi, K., K. Kasai and K. Ochi. 2004. Identification of the bacterial alarmone guanosine 5'-diphosphate 3'-diphosphate (ppGpp) in plants. Proc. Natl. Acad. Sci. USA. 101, 4320-4324
- Taylor, C.M., M. Beresford, H.A. Epton, D.C. Sigee, G. Shama, P.W. Andrew and I.S. Roberts. 2002. Listeria monocytogenes relA and hpt mutants are impaired in surface- attached growth and virulence. J. Bacteriol. 184, 621-628 https://doi.org/10.1128/JB.184.3.621-628.2002
- Toulokhonov, II, 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 https://doi.org/10.1074/jbc.M007184200
- van Delden, C., R. Comte and A.M. Bally. 2001. Stringent response activates quorum sensing and modulates cell density- dependent gene expression in Pseudomonas aeruginosa. J. Bacteriol. 183, 5376-5384 https://doi.org/10.1128/JB.183.18.5376-5384.2001
- van der Biezen, E.A., J. Sun, M.J. Coleman, M.J. Bibb and J.D. Jones. 2000. Arabidopsis RelA/SpoT homologs implicate (p)ppGpp in plant signaling. Proc. Natl. Acad. Sci. USA 97, 3747-3752
- Vrentas, C.E., T. Gaal, W. Ross, R.H. Ebright and R.L. Gourse. 2005. Response of RNA polymerase to ppGpp: requirement for the omega subunit and relief of this requirement by DksA. Genes. Dev. 19, 2378-2387 https://doi.org/10.1101/gad.1340305
- Wells, D.H. and S.R. Long. 2002. The Sinorhizobium meliloti stringent response affects multiple aspects of symbiosis. Mol Microbiol. 43, 1115-1127 https://doi.org/10.1046/j.1365-2958.2002.02826.x
- Wendrich, T.M., G. Blaha, D.N. Wilson, M.A. Marahiel and K.H. Nierhaus. 2002. Dissection of the mechanism for the stringent factor RelA. Mol. Cell 10, 779-788 https://doi.org/10.1016/S1097-2765(02)00656-1
- Xiao, H., M. Kalman, 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
- Zhang, G., E.A. Campbell, L. Minakhin, C. Richter, K. Severinov and S.A. Darst. 1999. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell 98, 811-824 https://doi.org/10.1016/S0092-8674(00)81515-9