Regulation of biosynthesis and transport of aromatic amino acids in low-GC Gram-positive bacteria

FEMS Microbiology Letters

Volumn 222, Issue 2, 2003, Pages 211-220

  Panina, Ekaterina M ^a   Vitreschak, Alexey G ^b,c   Mironov, Andrey A ^b,d   Gelfand, Mikhail S ^b,d  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Integrated Genomics   (Russian Federation)

^c INSTITUTE FOR INFORMATION TRANSMISSION PROBLEMS   (Russian Federation)

^d STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

Author keywords

ABC transporter; Aromatic amino acid; Regulation; T box; TRAP

Indexed keywords

2 DEHYDRO 3 DEOXYPHOSPHOHEPTONATE ALDOLASE; ABC TRANSPORTER; AMINO ACID TRANSPORTER; AROMATIC AMINO ACID; BACTERIAL DNA; BACTERIAL RNA; PHOSPHOTRANSFERASE; REGULATOR PROTEIN; SHIKIMIC ACID; T BOX TRANSCRIPTION FACTOR; TRYPTOPHAN TRANSPORTER; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; AMINO ACID TRANSPORT; ARTICLE; BACILLUS; BACTERIAL GENE; BACTERIAL GENOME; BACTERIAL METABOLISM; BIOSYNTHESIS; CLOSTRIDIUM; CONTROLLED STUDY; ENZYME SPECIFICITY; GENE CONTROL; GENE SEQUENCE; GRAM POSITIVE BACTERIUM; INTERMETHOD COMPARISON; LACTOCOCCUS; METABOLIC REGULATION; MOLECULAR PHYLOGENY; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN FAMILY; REGULATORY MECHANISM; REGULATORY SEQUENCE; SPECIES COMPARISON; STREPTOCOCCUS; TRANSCRIPTION REGULATION; TRANSLATION REGULATION;

CLOSTRIDIUM; FIRMICUTES; LACTOCOCCUS; POSIBACTERIA; STREPTOCOCCUS;

EID: 0037721512     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00303-3     Document Type: Article

References (20)

1. Pittard, A.J. (1996) Biosynthesis of aromatic amino acids. In: Escherichia coli and Salmonella. Cellular and Molecular Biology (Neidhardt, F.C. et al., Eds.), pp. 458-484. ASM Press, Washington, DC.
2. Sarsero J.P., Merino E., Yanofsky C. A Bacillus subtilis gene of previously unknown function, yhaG, is translationally regulated by tryptophan-activated TRAP and appears to be involved in tryptophan transport. J. Bacteriol. 182:2000;2329-2331.
3. Otwinowski Z., Schevitz R.W., Zhang R.G., Lawson C.L., Joachimiak A., Marmorstein R.Q., et al. Crystal structure of the trp repressor/operator complex at atomic resolution. Nature. 335:1988;321-329.
4. Pittard A.J., Davidson B.E. TyrR protein of Escherichia coli and its role as repressor and activator. Mol. Microbiol. 5:1991;1585-1592.
5. Jackson E.N., Yanofsky C. The region between the operator and first structural gene of the tryptophan operon of Escherichia coli may have a regulatory function. J. Mol. Biol. 76:1973;89-101.
6. Yanofsky C. Attenuation in the control of expression of bacterial operons. Nature. 289:1981;751-758.
7. Keller E.B., Calvo J. Alternative secondary structures of leader RNAs and the regulation of the trp, phe, his, thr, and leu operons. Proc. Natl. Acad. Sci. USA. 76:1979;6186-6190.
8. Terai, G., Takagi, T. and Nakai, K. (2001) Prediction of co-regulated genes in Bacillus subtilis on the basis of upstream elements conserved across three closely related species. Genome Biol. 11, research/0048.1.
9. Babitzke P., Gollnick P. Posttranscriptional initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure. J. Bacteriol. 183:2001;5795-5802.
10. Henkin T.M. tRNA-directed transcription antitermination. Mol. Microbiol. 13:1994;381-387.
11. Panina E.M., Vitreschak A.G., Mironov A.A., Gelfand M.S. Regulation of aromatic amino acid biosynthesis in gamma-proteobacteria. J. Mol. Microbiol. Biotechnol. 3:2001;529-543.
12. Schneider T.D., Stormo G.D., Gold L., Ehrenfeucht A. Information content of binding sites on nucleotide sequences. J. Mol. Biol. 188:1986;415-431.
13. Vitreshchak, A., Mironov, A.A. and Gelfand, M.S. (2001) Computer prediction of RNA secondary structure. The RNApattern program: searching for RNA secondary structure by the pattern rule. Proceedings 3rd Int. Conf. 'Complex Systems: Control and modeling problems', Samara, pp. 623-625.
14. Delorme C., Ehrlich S.D., Renault P. Regulation of expression of the Lactococcus lactis histidine operon. J. Bacteriol. 181:1999;2026-2037.
15. Grundy F.J., Haldeman M.T., Hornblow G.M., Ward J.M., Chalker A.F., Henkin T.M. The Staphylococcus aureus ileS gene, encoding isoleucyl-tRNA synthetase, is a member of the T-box family. J. Bacteriol. 179:1997;3767-3772.
16. Mironov A.A., Vinokurova N.P., Gelfand M.S. Software for analysis of bacterial genomes. Mol. Biol. (Moscow). 34:2000;222-231.
17. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgons D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:1997;4876-4882.
18. Felsenstein J. Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods. Methods Enzymol. 266:1996;418-427.
19. Green, J.M., Nichols, B.P. and Matthews, R.G. (1996) Folate biosynthesis, reduction, and polyglutamylation. In: Escherichia coli and Salmonella. Cellular and Molecular Biology (Neidhardt, F.C. et al., Eds.), pp. 665-673. ASM Press, Washington, DC.
20. Valbuzzi A., Yanofsky C. Inhibition of the B. subtilis regulatory protein TRAP by the TRAP-inhibitory protein, AT. Science. 293:2001;2057-2059.