NDLI: 'Activated'-RecA protein affinity chromatography of LexA repressor and other SOS-regulated proteins.

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'Activated'-RecA protein affinity chromatography of LexA repressor and other SOS-regulated proteins.

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'Activated'-RecA protein affinity chromatography of LexA repressor and other SOS-regulated proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mcentee, K. Freitag, N.
Description	Author Affiliation: Freitag N ( Laboratory of Biomedical and Environmental Sciences, School of Medicine, University of California, Los Angeles 90024.);
Abstract	We have developed an affinity column to study the interaction of LexA repressor and other substrates with the activated form of RecA protein. Nucleoprotein complexes of RecA protein, (dT)25-30, and adenosine 5'-[gamma-S]thio-triphosphate were formed in solution and bound to RecA protein-agarose columns. These 'activated'-RecA nucleoprotein complexes were retained by strong hydrophobic interactions. Purified LexA protein bound tightly to these activated RecA columns, whereas the LexA protein bound poorly to RecA-agarose alone. Once bound, LexA protein underwent specific proteolysis, and the fragments were released from the complex. The mutant LexA protein, LexA-SA119, which cannot carry out self-cleavage or RecA-mediated cleavage in solution, bound efficiently to the activated RecA column but was not cleaved, indicating that these columns can be used to identify residues involved in RecA-LexA binding. As an example of this use, nucleoprotein complexes were prepared using the RecA430 protein. In vivo the recA430 mutation blocks induction of the SOS response. LexA protein was not efficiently retained on the immobilized RecA430 complexes, suggesting that Gly-204 is required for efficient repressor binding. These results show that activated RecA affinity columns can be used to investigate the binding and cleaving properties of mutationally altered RecA and LexA proteins. Additionally, these activated RecA columns have been used to investigate binding interactions of phage lambda repressor, as well as the UmuC protein, which is required for chemical mutagenesis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism DNA Repair Escherichia Coli Proteins Rec A Recombinases Repressor Proteins SOS Response (Genetics) Serine Endopeptidases Transcription Factors Genetics Isolation & Purification Bacteriophage Lambda Chromatography, Affinity DNA-Directed DNA Polymerase Escherichia Coli Nucleoproteins Plasmids Protein Binding Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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