This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kline, B C Articles by Aleff, R A Search for Related Content PubMed PubMed Citation Articles by Kline, B C Articles by Aleff, R A

research-article

Site-specific proteolysis of mini-F plasmid replication protein RepE destroys initiator function and generates an incompatibility substance.

Department of Biochemistry and Molecular Biology, Mayo Clinic/Foundation, Rochester, Minnesota 55905.

ABSTRACT

Plasmid F replication is controlled by a plasmid-specified Rep protein with both autorepressor and initiator functions. The mechanism by which these two functions of a Rep protein are balanced to achieve stable replication is unknown; however, we speculated in prior work that Rep protein modification could be involved. We report here that naturally proteolyzed F RepE protein has been detected and characterized. The processed molecule lost the first 17 N-terminal aminoacyl residues and initiator function but acquired increased specific DNA-binding affinity in the presence of Escherichia coli chromosomal DNA. When supplied in trans, the altered protein acts as an incompatibility substance and eliminates maintenance of F'lac. These findings indicate that protein processing has the potential to contribute to the overall control of DNA replication.

This article has been cited by other articles:

• Nakamura, A., Wada, C., Miki, K. (2007). Structural basis for regulation of bifunctional roles in replication initiator protein. Proc. Natl. Acad. Sci. USA 104: 18484-18489 [Abstract] [Full Text]