JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Katayama, T
Right arrow Articles by Nagata, T
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Katayama, T
Right arrow Articles by Nagata, T
J Bacteriol. 1989 March; 171(3): 1485-1491

research-article

Genetic suppression of a dnaG mutation in Escherichia coli.

T Katayama, Y Murakami, C Wada, H Ohmori, T Yura and T Nagata

Institute for Virus Research, Kyoto University, Japan.

ABSTRACT

Escherichia coli strains with a temperature-sensitive mutation, dnaG2903, in the primase-encoding gene spontaneously reverted to the temperature-insensitive phenotype at a high frequency. Many of the reversions were caused by extragenic sdg suppressors. About 100 independently isolated sdg suppressors were analyzed. They fall into two classes. The sdgA mutations were genetically mapped very close to and upstream of the dnaG gene and were found to be cis dominant. DNA sequencing of two of them revealed that G----A and C----A base substitutions had occurred 43 and 62 bases, respectively, upstream of the dnaG start codon. This region represents a transcriptional terminator thought to contribute to control of dnaG gene expression. The other class of suppressor, sdgB, seemed to comprise mutant alleles in the rpoB gene coding for the beta subunit of RNA polymerase core enzyme. Some of them were initially isolated as rifampin-resistant mutants. Both the sdgA and sdgB suppressors were found to increase the transcriptional activity of dnaG. This finding and other observations led to the proposition that sdgA and sdgB suppress the phenotype caused by dnaG2903 by overproducing the mutated primase; the quantitative oversupply may compensate for the qualitative defect of the dnaG2903 primase. An alternative mechanism of suppression by sdgB is discussed.


J Bacteriol. 1989 March; 171(3): 1485-1491







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1989 by the American Society for Microbiology. All rights reserved.