We have cloned genes encoding RNase H from Escherichia coli rnh mutants, Salmonella typhimurium and Saccharomyces cerevisiae. Selection was accomplished by suppression of the temperature-sensitive growth phenotype of Escherichia coli strains containing the rnh-339::cat and either recB270 (Ts) or rec
Correlation of activity with phenotypes of Escherichia coli partial function mutants of rnh, the gene encoding RNase H
β Scribed by Itaya, Mitsuhiro ;Crouch, Robert J.
- Publisher
- Springer
- Year
- 1991
- Tongue
- English
- Weight
- 523 KB
- Volume
- 227
- Category
- Article
- ISSN
- 0026-8925
No coin nor oath required. For personal study only.
β¦ Synopsis
The rnh gene of Escherichia coli encodes RNase H. rnh mutants display at least two phenotypes: (1) they require functional RecBCD enzyme for growth; thus rnh-339::cat recB270 (Ts) and rnh-339::cat recC271 (Ts) strains are temperature sensitive for growth; (2) rnh mutants permit replication that is independent of the chromosomal origin, presumably by failing to remove RNA-DNA hybrids from which extra-original replication can be primed. We report here that manifestation of these two phenotypes occurs at different levels of RNase H function; we have examined partially functional rnh mutants for their in vitro RNase H activity, their ability to rescue viability in recB or recC cells and their ability to permit growth of mutants incapable of using oriC [dnaA (Ts)].
π SIMILAR VOLUMES
A series of temperature-resistant revertants were isolated from strains of Escherichia coli K12 carrying a temperature-sensitive mutation in the dnaA gene. Four independent revertants were found which still carry the original ts mutation. The ability of these strains to grow at high temperature is d
In order to select mutants that would help to characterize the post-transcriptional regulation of rpsA, we constructed a strain in which the growth rate on lactose minimal medium is determined by the amount of an rpsA-lacZ' alpha-fragment fusion protein produced, even when this is encoded by a high-