Kinetic mechanism of nucleotide binding toEscherichia coli transcription termination factor Rho: Stopped-flow kinetic studies using ATP and fluorescent ATP analogues-Reference-Cited by-同舟云学术

Kinetic mechanism of nucleotide binding toEscherichia coli transcription termination factor Rho: Stopped-flow kinetic studies using ATP and fluorescent ATP analogues

Published:2004-02 Issue:1 Volume:9 Page:23-34
ISSN:1226-8372
Container-title:Biotechnology and Bioprocess Engineering
language:en
Short-container-title:Biotechnol Bioproc E

Author:

Kim Dong-Eun

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/BF02949318.pdf

Reference29 articles.

1. Brennan, C. A., A. J. Dombroski, and T. Platt (1987) Transcription termination factor rho is an RNA-DNA helicase.Cell 48: 945–952.

2. Geiselmann, J., Y. Wang, S. E. von Seifried, and P. H. Hippel (1993) A physical model for the translocation and helicase activities ofEscherichia coli transcription termination protein Rho.Proc. Natl. Acad. Sci. USA 90: 7754–7758.

3. Richardson, J. P. (1996) Structural organization of transcription termination factor Rho.J. Biol. Chem. 271: 1251–1254.

4. Stitt, B. L. (1988)Escherichia coli transcription termination protein rho has three hydrolytic sites for ATP.J. Biol. Chem. 263: 11130–11137.

5. Geiselmann, J. and P. H. von Hippel (1992). Functional interactions of ligand cofactorswithEscherichia coli transcription termination factor rho: I. Binding of ATP.Protein Sci. 1: 850–860.

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