Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme

Biochemistry

Volumn 47, Issue 6, 2008, Pages 1518-1531

  Mitra, Ashima ^a   Sarma, Siddhartha P ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

FAD BINDING; POLYPEPTIDE FRAGMENTS; SIDE CHAIN;

BINDING SITES; CHEMICAL SHIFT; DICHROISM; ENZYME ACTIVITY; POLYPEPTIDES;

ESCHERICHIA COLI;

ACETOLACTATE SYNTHASE; FLAVINE ADENINE NUCLEOTIDE;

ARTICLE; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS;

ACETOLACTATE SYNTHASE; AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CIRCULAR DICHROISM; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLAVIN-ADENINE DINUCLEOTIDE; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

ESCHERICHIA COLI;

EID: 38949122375     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701893b     Document Type: Article

References (65)

1. Umbarger, H. E., and Brown, B. (1958) Isoleucine and valine metabolism in Escherichia coli, J. Biol. Chem. 233, 1156-1160.
2. Chipman, D. M., Duggleby, R. G., and Tittmann, K. (2005) Mechanisms of acetohydroxyacid synthases, Curr. Opin. Chem. Biol. 9, 475-481.
3. Chipman, D. M., Barak, Z., and Schloss, J. V. (1998) Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases, Biochim. Biophys. Acta 1385, 401-419.
4. Umbarger, H. E. (1987) Biosynthesis of Branched-Chain Amino Acids, in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F. C., Ed.) pp 352-367, American Society for Microbiology, Washington, DC.
5. Barak, Z., Chipman, D. M., and Gollop, N. (1987) Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria, J. Bacteriol. 169, 3750-3756.
6. Dailey, F. E., and Cronan, J. E. J. (1986) Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source, J. Bacteriol. 165, 453-460.
7. Eoyang, L., and Silverman, P. M. (1984) Purification and subunit composition of acetohydroxyacid synthase I from Escherichia coli K-12, J. Bacteriol. 157, 184-189.
8. Hill, C. M., Pang, S. S., and Duggleby, R. G. (1997) Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits, Biochem. J. 327, 891-898.
9. Vyazmensky, M., Sella, C., Barak, Z., and Chipman, D. M. (1996) Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme, Biochemistry 35, 10339-10346.
10. Grimminger, H., and Umbarger, H. E. (1978) Acetohydroxy acid synthase I of Escherichia coli: purification and properties, J. Biol. Chem. 137, 846-853.
11. Davis, E. J., Blatt, J. M., Henderson, E. K., Whittaker, J. J., and Jackson, J. H. (1977) Valine-sensitive acetohydroxy acid synthases in Escherichia coli K-12: Unique regulation modulated by multiple genetic sites, Mol. Gen. Genet. 156, 239-249.
12. Vinogradov, V., Vyazmensky, M., Engel, S., Belenky, I., Kaplun, A., Kryukov, O., Barak, Z., and Chipman, D. M. (2006) Acetohydroxy acid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties, Biochim. Biophys. Acta 1760, 356-363.
13. Favre, R., Wiater, A., Puppo, S., Iaccarino, M., Noelle, R., and Freundlich, M. (1976) Expression of a valine-resistant acetolactate synthase activity mediated by the ilv O and ilv G genes of Escherichia coli K-12, Mol. Gen. Genet. 143, 243-252.
14. Wek, R. C., Hauser, C. A., and Hatfield, G. W. (1985) The nucleotide sequence of the ilvBN operon of Escherichia coli: sequence homologies of the acetohydroxy acid synthase isozymes, Nucleic Acids Res. 13, 3995-4010.
15. Lawther, R. P., Wek, R. C., Lopes, J. M., Perira, R., Taillon, B. E., and Wesley, G. (1987) The complete nucleotide sequence of the ilvGMEDA Operon of Escherichia Coli K-12, Nucleic Acids Res. 15, 2137-2155.
16. Squires, C. H., DeFelice, M., Devereux, J., and Calvo, J. M. (1983) Molecular structure of ilvIH and its evolutionary relationship to ilvG in Escherichia coli K12, Nucleic Acids Res. 11, 5299-5313.
17. Eoyang, L., and Silverman, P. M. (1986) Role of small subunit (IlvN polypeptide) of acetohydroxyacid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition, J. Bacteriol. 166, 901-904.
18. Vyazmensky, M., Elkayam, T., Chipman, D. M., and Barak, Z. (2000) Isolation of subunits of acetohydroxy acid synthase III and reconstitution of holoenzyme, Methods Enzymol. 324, 95-203.
19. Pang, S. S., and Duggleby, R. G. (1999) Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase, Biochemistry 38, 5222-5231.
20. Lee, Y., and Duggleby, R. G. (2001) Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit, Biochemistry 40, 6836-6844.
21. Gollop, N., Damri, D., Barak, Z., and Chipman, D. M. (1989) Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli, Biochemistry 28, 6310-6317.
22. Pang, S. S., Duggleby, R. G., and Guddat, L. W. (2002) Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors, J. Mol. Biol. 317, 249-262.
23. Pang, S. S., Guddat, L. W., and Duggleby, R. G. (2001) Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroxyacid synthase, Acta Crystallogr. D57, 1321-1323.
24. Kaplun, A., Vyazmensky, M., Zherdev, Y., Belenky, I., Slutzker, A., Mendel, S., Barak, Z., Chipman, D. M., and Shannan, B. (2006) Structure of the regulatory subunit of acetohydroxy acid synthase isozyme III from Escherichia coli. J. Mol. Biol. 357, 951-963.
25. Mendel, S., Elkayam, T., Sella, C., Vinogradov, V., Vyazmensky, M., Chipman, D. M., and Barak, Z. (2001) Acetohydroxyacid synthase:A proposed structure for the regulatory subunits supported by evidence from mutagenesis, J. Mol. Biol. 307, 465-477.
26. Mendel, S., Vinogradov, V., Vyazmensky, M., Chipman, D. M., and Barak, Z. (2003) The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli, J. Mol. Biol. 325, 275-284.
27. Vyazmensky, M., Engel, S., Kryukov, O., Berkovich-Berger, D., and Kaplun, L. (2006) Construction of an active acetohydroxyacid synthase I with a flexible linker connecting the catalytic and the regulatory subunits, Biochim. Biophys. Acta 1764, 955-960.
28. 5 as a fusion host, Protein Expression Purif. 41, 84-97.
29. Mori, S., Abeygunawardana, C., Johnson, M. O., and Zijl, P. C. M. V. (1995) Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation, J. Magn. Reson. B 108, 94-98.
30. Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
31. 2H-decoupling, J. Am. Chem. Soc. 118, 6570-6579.
32. Wittekind, M., and Mueller, L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins, J. Magn. Reson. B 101, 201-205.
33. Grzesiek, S., and Bax, A. (1992) Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein, J. Magn. Reson. 96, 432-440.
34. Muhandiram, D. R., and Kay, L. E. (1994) Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity, J. Magn. Reson. 193, 203-216.
35. Pervushin, K. (2000) Impact of Transverse Relaxation Optimized Spectroscopy (TROSY) on NMR as a technique in structural biology, Q. Rev. Biophys. 33, 161-197.
36. Salzmann, M., Pervushin, K., Wagner, G., Senn, H., and Wuthrich, K. (1998) TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins, Proc. Natl. Acad. Sci. U.S.A. 95, 13585-13590.
37. Eletsky, A., Kienhöfer, A., and Pervushin, K. (2001) TROSY NMR with partially deuterated proteins, J. Biomol. NMR 20, 177-180.
38. Marion, D., Ikura, M., Tschudin, R., and Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85, 393-399.
39. 15N-Labeled Proteins, J. Am. Chem. Soc. 111, 1515-1517.
40. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
41. Kraulis, P. J. (1989) ANSIG: a program for the assignment of protein 1H 2D NMR spectra by interactive graphics, J. Magn. Reson. 84, 627-633.
42. Kraulis Domaille, P. J., Campbell-Burk, S. L., Van Aken T., and Laue, E. D. (1994) Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and fourdimensional NMR spectroscopy, Biochemistry 33, 3515-3531.
43. Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD - Visual Molecular Dynamics, J. Mol. Graphics 14, 33-38.
44. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
45. Westerfeld, W. W. (1945) A colorimetric determination of blood acetoin, J. Biol. Chem. 161, 495-502.
46. Epelbaum, S., Chipman, D. M., and Barak, Z. (1990) Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited, Anal. Biochem. 191, 96-99.
47. Vinogradov, M., Kaplun, A., Vyazmensky, M., Engel, S., Globik, R., Tittmann, K., Uhlemann, K., Meshalkina, L., Barak, L., Hubner, G., and Chipman, D. M. (2005) Monitoring the acetohydroxy acid synthase reaction and related carboligations by circular dichroism spectroscopy, Anal. Biochem. 342, 126-133.
48. Nemeria, N., Tittmann, K., Joseph, E., Zhou, L., Vazquez-Coll, M. B., Arjunan, P., Hubner, G., Furey, W., and Jordan, F. (2005) Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in the active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity, J. Biol. Chem. 280, 21473-21482.
49. Golovanov, A. P., Hautbergue, M. G., Wilson, A. S., and Lian, L. (2004) A simple method for improving protein solubility and long-term stability, J. Am. Chem. Soc. 126, 8933-8939.
50. Anglister, J., Grzesiek, S., Ren, H., Klee, C. B., and Bax, A. (1993) Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS, J. Biomol. NMR 3, 121-126.
51. Clore, G. M., Wingfield, P. T., and Gronenborn, A. M. (1991) High-resolution three-dimensional structure of Interleukin 1β in solution by three- and four-dimensional Nuclear Magnetic Resonance Spectroscopy, Biochemistry 30, 2315-2323.
52. l, an inhibitor of programmed cell death, Nature 381, 335-341.
53. Wang, G., Peterkofsky, A., Keifer, P. A., and Li, X. (2005) NMR characterization of the Escherichia coli nitrogen regulatory protein IIA Ntr in solution and interaction with its partner protein, Npr, Protein Sci. 14, 1082-1090.
54. Pérez-Cañadillas, J. M., Santoro, J., Campos-Olivas, R., Lacadena, J., Pozo, A. M., Gavilanes, J. G., Rico, M., and Bruix, M. (2000) The highly refined solution structure of the cytotoxic ribonuclease α-Sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity, J. Mol. Biol. 299, 1061-1073.
55. 13C Nuclear Magnetic Resonance chemical shifts, J. Am. Chem. Soc. 113, 5490-5492.
56. Abell, L. M., and J. V. Schloss. (1991) Oxygenase side reactions of acetolactate synthase and other carbanion-forming enzymes, Biochemistry 30, 7883-7887.
57. Tse, J. M. T., and Schloss, J. V. (1993) The oxygenase reaction of Acetolactate Synthase, Biochemistry 32, 10398-10403.
58. Grandoni, J. A., Peter, M. T., and Schloss, J. V. (1998) Inhibitors of branched-chain amino acid biosynthesis as potential antituberculosis agents, J. Antimicrob. Chemother. 42, 475-482.
59. Sahm, H., and Eggeling, L. (1999) Construction of L-Isoleucine overproducing strains of Corynebacterium glutamicum, Naturwissenschaften 86, 33-38.
60. Eggeling, I., Cordes, C., Eggeling, L., and Sahm, H. (1987) Regulation of acetohydroxy acid synthase in Corynebacterium glutamicum during fermentation of α-ketobutyrate to L-isoleucine, Appl. Microbiol. Biotechnol. 25, 346-351.
61. Kang, C., Kim, S., and Fromm, H. J. (1998) Subunit complementation of Escherichia coli Adenylosuccinate Synthetase, J. Biol. Chem. 271, 29722-29728.
62. Wente, S. R., and Schachman, H. K. (1987) Shared active sites in oligomeric enzymes: Model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis, Proc. Natl. Acad. Sci. U.S.A. 84, 31-35.
63. Tarun, A. S., and Theologis, A. (1998) Complementation analysis of mutants of 1-aminocyclopropane-1-carboxylate synthase reveals the enzyme is a dimer with shared active sites, J. Biol. Chem. 20, 12509-12514.
64. Schobert, B., and Tschesche, H. (1978) Unusual solution properties of proline and its interaction with proteins, Biochim. Biophys. Acta 541, 270-277.
65. Samuel, D., Kumar, T. K., Ganesh, G., Jayaraman, G., Yang, P. W., Chang, M. M., Trivedi, V. D., Wang, S. L., Hwang, K. C., Chang, D. K., and Yu, C. (2000) Proline inhibits aggregation during protein refolding, Protein Sci. 9, 344-352.