RecA, Tus protein and constitutive stable DNA replication inEscherichia coli rnhA mutants
Autor: | Tokio Kogoma, Xiankang Hong, Kathryn G. Barnard |
---|---|
Rok vydání: | 1994 |
Předmět: |
DNA Replication
DNA Bacterial Ribonuclease H Mutant Biology medicine.disease_cause chemistry.chemical_compound Bacterial Proteins Escherichia coli Genetics medicine Molecular Biology Gene Recombination Genetic Mutation Recombinase activity Escherichia coli Proteins DNA replication Chromosomes Bacterial Rec A Recombinases chemistry Genes Bacterial DNA Nucleotidyltransferases Nucleic Acid Conformation Homologous recombination DNA |
Zdroj: | Molecular and General Genetics MGG. 244:557-562 |
ISSN: | 1432-1874 0026-8925 |
DOI: | 10.1007/bf00583907 |
Popis: | Constitutive stable DNA replication (cSDR), which uniquely occurs in Escherichia coli rnhA mutants deficient in ribonuclease HI activity, requires RecA function. The recA428 mutation, which inactivates the recombinase activity but imparts a constitutive coprotease activity, blocks cSDR in rnhA mutants. The result indicates that the recombinase activity of RecA, which promotes homologous pairing and strand exchange, is essential for cSDR. Despite the requirement for RecA recombinase activity, mutations in recB, recD, recJ, ruvA and ruvC neither inhibit nor stimulate cSDR. It was proposed that the property of RecA essential for homologous pairing and strand exchange is uniquely required for initiation of cSDR in rnhA mutants without involving the homologous recombination process. The possibility that RecA protein is necessary to counteract the action of Tus protein, a contra-helicase which stalls replication forks in the ter region of the chromosome, was ruled out because introduction of the tus::kan mutation, which inactivates Tus protein, did not alleviate the RecA requirement for cSDR. |
Databáze: | OpenAIRE |
Externí odkaz: |