Cloning, expression, purification, and characterization of Vibrio cholerae transcriptional activator, HlyU

Protein Expression and Purification

Volumn 48, Issue 1, 2006, Pages 118-125

  Saha, Rudra Prasad ^a   Basu, Gautam ^a   Chakrabarti, Pinak ^a  

^a BOSE INSTITUTE   (India)

Author keywords

Circular dichroism spectroscopy; Fluorescence spectroscopy; Haemolysin; HlyU protein; Transcriptional regulation; Virulence

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); BACTERIAL PROTEIN; CYSTEINE; GUANIDINE; HLYU PROTEIN, VIBRIO CHOLERAE; SOLVENT; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR;

ARTICLE; BIOLOGICAL MODEL; CHEMISTRY; CIRCULAR DICHROISM; ESCHERICHIA COLI; GEL CHROMATOGRAPHY; GENETIC TRANSCRIPTION; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; PROTEIN FOLDING; SPECTROFLUOROMETRY; VIBRIO CHOLERAE;

BACTERIAL PROTEINS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CLONING, MOLECULAR; CYSTEINE; DITHIONITROBENZOIC ACID; ESCHERICHIA COLI; GUANIDINE; MODELS, GENETIC; PROTEIN FOLDING; SOLVENTS; SPECTROMETRY, FLUORESCENCE; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC; VIBRIO CHOLERAE;

ESCHERICHIA COLI; VIBRIO CHOLERAE;

EID: 33646879576     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.02.008     Document Type: Article

References (13)

1. Finkelstein R.A. Cholera. Crit. Rev. Microbiol. 2 (1973) 553-623
2. DiRita V.J. Multiple regulatory systems in Vibrio cholerae. Trends Microbiol. 2 (1994) 37-38
3. Williams S.G., Attridge S.R., and Manning P.A. The transcriptional activator HlyU of Vibrio cholerae; nucleoside sequence and role in virulence gene expression. Mol. Microbiol. 9 (1993) 751-760
4. Williams S.G., and Manning P.A. Transcription of the Vibrio cholerae haemolysin gene, hlyA, and cloning of a positive regulatory locus, hlyU. Mol. Microbiol. 5 (1991) 2031-2038
5. Kim Y.R., Lee S.E., Kim C.M., Kim S.Y., Shin E.K., Shin D.H., Chung S.S., Choy H.E., Progulske-Fox A., Hillman J.D., Handfield M., and Rhee J.H. Characterization and pathogenic significance of Vibrio vulnificus antigens preferentially expressed in septicemic patients. Infect. Immun. 71 (2003) 5461-5471
6. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82 (1959) 70-77
7. Pace C.N., and Shaw K.L. Linear extrapolation method of analyzing solvent denaturation curves. Proteins Suppl. 4 (2000) 1-7
8. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., and Bairoch A. Protein identification and analysis tools on the ExPASy server. In: Walker J.M. (Ed). The Proteomics Protocols Handbook (2005), Humana Press 571-607
9. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
10. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
11. Andrade M.A., Chacon P., Merelo J.J., and Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
12. Bohm G., Muhr R., and Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5 (1992) 191-195
13. Vivian J.T., and Callis P.R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80 (2001) 2093-2109