Constitutive mutations in the Escherichia coli AraC protein

Journal of Bacteriology

Volumn 191, Issue 8, 2009, Pages 2668-2674

  Dirla, Stephanie ^a   Chien, John Yeh Heng ^a   Schleif, Robert ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARABINOSE; ARAC PROTEIN; CHYMOTRYPSIN; CORE PROTEIN; CYSTEINE; FUCOSE; TRYPSIN; ARAC PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIAL METABOLISM; BETA SHEET; CIRCULAR DICHROISM; DIMERIZATION; ESCHERICHIA COLI; FLUORESCENCE; GENE MUTATION; GENE REPRESSION; GENE STRUCTURE; GENETIC STABILITY; IMMUNOREACTIVITY; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; AMINO ACID SUBSTITUTION; BIOLOGICAL MODEL; BIOSYNTHESIS; CHEMICAL STRUCTURE; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MISSENSE MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE;

ESCHERICHIA COLI;

AMINO ACID SUBSTITUTION; ARABINOSE; ARAC TRANSCRIPTION FACTOR; CHYMOTRYPSIN; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FUCOSE; GENE EXPRESSION REGULATION, BACTERIAL; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION, MISSENSE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; TRYPSIN;

EID: 65249161570     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01529-08     Document Type: Article

References (28)

1. Beverin, S., D. E. Sheppard, and S. S. Park. 1971. d-Fucose as a gratuitous inducer of the arabinose operon in strains of Escherichia coli B/r mutant in gene araC. J. Bacteriol. 107:79-86.
2. Carra, J., and R. Schleif. 1993. Variation of half-site organization and DNA looping by AraC protein. EMBO J. 12:35-44.
3. Dunn, T., S. Hahn, S. Ogden, and R. Schleif. 1984. An operator at -280 base pairs that is required for repression of araBAD operon promoter: addition of DNA helical turns between the operator and promoter cyclically hinders repression. Proc. Natl. Acad. Sci. USA 81:5017-5020.
4. Englesberg, E., J. Irr, J. Power, and N. Lee. 1965. Positive control of enzyme synthesis by gene C in the arabinose system. J. Bacteriol. 90:946-957.
5. Ghosh, M., and R. R. Schleif. 2001. Biophysical evidence of arm-domain interactions in AraC. Anal. Biochem. 295:107-112.
6. Gill, S. C., and P. H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 189:319-326.
7. Gryczynski, U., and R. Schleif. 2004. A portable allosteric mechanism. Proteins 57:9-11.
8. Hahn, S., T. Dunn, and R. F. Schleif. 1984. Upstream repression and CRP stimulation of the Escherichia coli arabinose operon. J. Mol. Biol. 180:61-72.
9. Harmer, T., M. Wu, and R. Schleif. 2001. The role of rigidity in DNA looping-unlooping by AraC. Proc. Natl. Acad. Sci. USA 98:427-431.
10. Hubbard, S. J., F. Eisenmenger, and J. M. Thornton. 1994. Modelingstudies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 3:757-768.
11. Lobell, R., and R. Schleif. 1990. DNA looping and unlooping by AraC protein. Science 250:528-532.
12. LaRonde-LeBlanc, N., and C. Wolberger. 2000. Characterization of the oli- gomeric states of wild and mutant AraC. Biochemistry 39:11593-11601.
13. MacInnes, K. R., D. E. Sheppard, and B. Falgout. 1978. Regulatory properties of araC (c) mutants in the arabinose operon of Escherichia coli B/r. J. Bacteriol. 133:178-184.
14. Martin, K., L. Huo, and R. Schleif. 1986. The DNA loop model for ara repression: AraC protein occupies the proposed loop sites in vivo and repression-negative mutations lie in these same sites. Proc. Natl. Acad. Sci. USA 83:3654-3658.
15. Nathanson, N. M., and R. Schleif. 1975. Paucity of sites mutable to constitutivity in the araC activator gene of the arabinose operon of Escherichia coli. J. Mol. Biol. 25:185-199.
16. Reed, W., and R. Schleif. 1999. Hemiplegic mutations in AraC protein. J. Mol. Biol. 294:417-425.
17. Ross, J. J., U. Gryczynski, and R. Schleif. 2003. Mutational analysis of residue roles in AraC function. J. Mol. Biol. 328:85-93.
18. Rodgers, M. E., N. D. Holder, S. Dirla, and R. Schleif. 2009. Functional modes of the regulatory arm of AraC. Proteins 74:81-91.
19. Saviola, B., R. Seabold, and R. F. Schleif. 1998. Arm-domain interactions in AraC. J. Mol. Biol. 289:539-548.
20. Schleif, R. F., and P. C. Wensink. 1981. Practical methods in molecular biology. Springer-Verlag, New York, NY.
21. Seabold, R., and R. Schleif. 1998. Apo-AraC actively seeks to loop. J. Mol. Biol. 278:529-538.
22. Sheppard, D. E. 1986. Dominance relationships among mutant alleles of regulatory gene araC in the Escherichia coli B/R arabinose operon. J. Bac- teriol. 168:999-1001.
23. Soisson, S., B. MacDougal-Shackleton, R. Schleif, and C. Wolberger. 1997. Structural basis for ligand-regulated oligomerization of AraC. Science 276: 421-425.
24. Timmes, A., M. Rodgers, and R. Schleif. 2004. Biochemical and physiological properties of the DNA binding domain of AraC protein. J. Mol. Biol. 340:731-738.
25. Weldon, J. E., M. Rodgers, C. Larkin, and R. Schleif. 2007. Structure and properties of a truely apo form of AraC dimerization domain. Proteins 66:646-654.
26. Wu, M., and R. Schleif. 2001. Mapping arm-DNA-binding domain interactions in AraC. J. Mol. Biol. 307:1001-1009.
27. Wu, M., and R. Schleif. 2001. Strengthened arm-dimerization domain interactions in AraC. J. Biol. Chem. 276:2562-2564.
28. Zhang, X., T. Reeder, and R. Schleif. 1996. Transcription activation parameters at ara pBAD. J. Mol. Biol. 258:14-24.