Identification of an Indispensable Amino Acid for ppGpp Synthesis of Escherichia coli SpoT Protein

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 12, 2002, Pages 2735-2738

  Fujita, Chizuko ^a   Maeda, Maki ^a   Fujii, Takako ^a   Iwamoto, Ryoko ^a   Ikehara, Kenji ^a  

^a NARA WOMEN'S UNIVERSITY   (Japan)

Author keywords

Amino acid substitution; Catalytic center; Ppgpp synthesis; SpoT protein; Stringent response

Indexed keywords

ALANINE; ASPARTIC ACID; GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; GUANOSINE 3',5' BIS(DIPHOSPHATE) 3' PYROPHOSPHATASE; GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHATASE; INORGANIC PYROPHOSPHATASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOSYNTHESIS; CELL DIVISION; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MOLECULAR GENETICS; MUTATION;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; CELL DIVISION; ESCHERICHIA COLI; GUANOSINE TETRAPHOSPHATE; MOLECULAR SEQUENCE DATA; MUTATION; PYROPHOSPHATASES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0042201888     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.2735     Document Type: Article

References (34)

1. Cashel, M., Gentry, D. R., Hernandez, V. J., and Vinella, D., The stringent response. In “Escherichia coli and Salmonella typhimulium: cellular and molecular biology” 2nd ed. vol. 2, eds. Neidhardt, F. C., Curtis, R., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E., ASM Press, Washington, D.C., pp. 1458-1496 (1996).
2. Justesen, J., Lund, T., Pedersen, F. S., and Kjeldgaard, N. O., The physiology of stringent factor (ATP:GTP 3'-diphosphotransferase) in Escherichia coli. Biochimie, 68, 715-722 (1986).
3. An, G., Justesen, J., Watson, R. J., and Friesen, J. D., Cloning the spoT gene of Escherichia coli: identification of the spoT gene product. J. Bacteriol., 137, 1100-1110 (1979).
4. Sy, J., In vitro degradation of guanosine 5'-diphosphate 3'-diphosphate. Proc. Natl. Acad. Sci. USA, 74, 5529-5533 (1977).
5. Metzger, S., Schreiber, G., Aizenman, E., Cashel, M., and Glaser, G., Characterization of the relA1 mutation and a comparison of relA1 with new relA null alleles in Escherichia coli. J. Biol. Chem., 264, 21146-21152 (1989).
6. Sarubbi, E., Rudd, K., Xiao, H., Ikehara, K., Kalman, M., and Cashel, M., Characterization of the spoT gene Escherichia coli. J. Biol. Chem., 264, 15074-15082 (1989).
7. Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G., and Cashel, M., Residual guanosine 3',5’-bipyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J. Biol. Chem., 266, 5980-5990 (1991).
8. Wendrich, T. M., and Marahiel, M. A., Cloning and characterization of a relA /spoT homologue from Bacillus subtilis. Mol. Microbiol., 26, 65-79 (1997).
9. Mechold, U., Cashel, M., Steiner, K., Gentry, D., and Malke, H., Functional analysis of a relAsspoT gene homolog from Streptococcus equisimilis. J. Bacteriol., 178, 1401-1411 (1996).
10. Chakraburtty, R., White, J., Takano, E., and Bibb, M., Cloning, characterization and disruption of a (p)ppGpp synthetase gene (relA) of Streptomyces colelicolor A3(2). Mol. Microbiol., 19, 357-368 (1996).
11. Jones, G. H., Activation of ATP:GTP 3'-pyrophosphotransferase (guanosine pentaphosphate synthetase) in Streptomyces antibioticus. J. Bac-teriol., 176, 1482-1487 (1994).
12. Jones, G. H., Purification and properties of ATP:GTP 3'-pyrophosphotransferase (guanosine pentaphosphate synthetase) in Streptomyces anti-bioticus. J. Bacteriol., 176, 1475-1481 (1994).
13. Flarch, K., Axberg, T., Albertson, N. H., and Kjelleberg, S., Stringent control during carbon starvation of marine Vibrio sp. Strain S14: molecular cloning, nucleotide sequence, and deletion of relA gene. J. Bacteriol., 176, 5949-5957 (1994).
14. Gentry, D. R., and Cashel, M., Mutational analysis of the Escherichia coli spoT gene identified distinct overlapping regions involved in ppGpp synthesis and degradation. Mol. Microbiol., 19, 1373-1384 (1996).
15. Martinez-Costa, O. H., Fernandez-Moreno, M. A., and Malpartida, F., The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp synthesizing and-degrading activities. J. Bacteriol., 180, 4123-4132 (1998).
16. Mayans, O., Ivens, A., Nissen, L. J., Kirschner, K., and Wilmanns, M., Structural analysis of two enzymes catalyzing reverse metabolic reactions implies common ancestry. EMBO J., 21, 3245-3254 (2002).
17. Shimba, N., Shinohara, M., Yokoyama, K., Kashiwagi, T., Ishikawa, K., Ejima, D., and Suzuki, E., Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Lett., 517, 175-179 (2002).
18. Eaton, J. T., Naylor, C. E., Howells, A. M., Moss, D. S., Titball, R. W., and Basak, A. K., Crystal structure of the C. perfringens alpha-toxin with the active site closed by a flexible loop region. J. Mol. Biol., 319, 275-281 (2002).
19. Kimura, M., Furuichi, M., Yamamoto, M., Kumasaka, T., Mizuno, H., Miyano, M., and Yamaguchi, I., The flexible C-terminal region of Aspergillus terreus blasticidin S deaminase: identification of its functional roles with deletion enzymes. Biochem. Biophys. Res. Commun., 290, 421-426 (2002).
20. Haruyama, K., Nakai, T., Miyahara, I., Hirotsu, K., Mizuguchi, H., Hayashi, H., and Kagamiyama, H., Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5?-phosphopyridoxyl)-L-gluta-mate: double substrate recognition of the enzyme. Biochemistry, 40, 4633-4644 (2001).
21. Sam, M. D., and Perona, J. J., Catalytic roles of divalent metal ions in phosphoryl transfer by EcoRV endonuclease. Biochemistry, 38, 6576-6586 (1999).
22. Focia, P. J., Craig, S. P., and Eakin, A. E., Approaching the transition state in the crystal structure of a phosphoribosyltransferase. Biochemistry, 37, 17120-17127 (1998).
23. Cochran, J. W., and Byrne, R. W., Isolation and properties of a ribosome-bound factor required for ppGpp and ppGpp synthesis in Escherichia coli. J. Biol. Chem., 249, 353-360 (1974).
24. Lipmann, F., and Sy, J., The enzymic mechanism of guanosine 5',3'-popyphosphate synthesis. Prog. Nucl. Acid Res. Mol. Biol., 17, 1-14 (1976).
25. Fujita, C., Nishimura, A., Iwamoto, R., and Ikehara, K., Guanosine 5?-diphosphate 3?-diphosphate (ppGpp) synthetic activities on Escherichia coli SpoT domains. Biosci. Biotechnol. Bichem., 66, 1515-1523 (2002).
26. Deng, W. P., and Nickoloff, L. A., Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem., 200, 81-88 (1992).
27. Miller, J. H., Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, New York (1972).
28. Neidhardt, F. C., Bloch, P. L., and Smith, D. F., Culture medium for Enterobacteria. J. Bacteriol., 119, 736-746 (1974).
29. Spira, B., and Yagil, E., The relation between ppGpp and the PHO regulon in Escherichia coli. Mol. Gen. Genet., 257, 469-477 (1998).
30. Davis, R. W., Botstein, D., and Roth, J. R., Advanced bacterial genetics. Cold Spring Harbor Laboratory Press, New York (1980).
31. Ikehara, K., Ando, H., Takada, Y., and Sugae, K., Presence of guanosine 5?-diphosphate 3?-diphosphate in Bacillus subtilis vegetative cells. J. Biochem., 89, 511-516 (1981).
32. s is positively regulated by ppGpp. J. Bacteriol., 175, 7982-7989 (1993).
33. Bochner, B. R., and Ames, B. R., Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J. Biol. Chem., 257, 9759-9769 (1982).
34. Gropp, M., Strausz, Y., Gross, M., and Glaser, G., Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain. J. Bacteriol., 183, 570-579 (2001).