RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation.
- 1 March 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (6), 1816-1820
- https://doi.org/10.1073/pnas.85.6.1816
Abstract
The products of the SOS-regulated umuDC operon are required for most UV and chemical mutagenesis in Escherichia coli. It has been shown that the UmuD protein shares homology with LexA, the repressor of the SOS genes. In this paper we describe a series of genetic experiments that indicate that the purpose of RecA-mediated cleavage of UmuD at its bond between Cys-24 and Gly-25 is to activate UmuD for its role in mutagenesis and that the COOH-terminal fragment of UmuD is necessary and sufficient for the role of UmuD in UV mutagenesis. Other genetic experiments are presented that (i) support the hypothesis that the primary role of Ser-60 in UmuD function is to act as a nucleophile in the RecA-mediated cleavage reaction and (ii) raise the possibility that RecA has a third role in UV mutagenesis besides mediating the cleavage of LexA and UmuD.This publication has 42 references indexed in Scilit:
- UmuD mutagenesis protein of Escherichia coli: overproduction, purification, and cleavage by RecA.Proceedings of the National Academy of Sciences, 1988
- Cleavage of the lambda and P22 repressors by recA protein.Journal of Biological Chemistry, 1982
- Inducibility of a gene product required for UV and chemical mutagenesis in Escherichia coli.Proceedings of the National Academy of Sciences, 1981
- Identification of the uvrA gene productJournal of Molecular Biology, 1981
- Two mutations that alter the regulatory activity of E. coli recA proteinNature, 1981
- Cleavage of the Escherichia coli lexA protein by the recA protease.Proceedings of the National Academy of Sciences, 1980
- Escherichia coli recA gene product inactivates phage lambda repressor.Proceedings of the National Academy of Sciences, 1978
- Uvm mutants of Escherichia coli K 12 deficient in UV mutagenesisMolecular Genetics and Genomics, 1978
- Isolation and characterization of mutants of Escherichia coli deficient in induction of mutations by ultraviolet lightMolecular Genetics and Genomics, 1977
- Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteasesBiochemistry, 1973