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

B. C. Kline, G. S. Sandhu, B. W. Eckloff, R. A. Aleff

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)3004-3010
Number of pages7
JournalJournal of Bacteriology
Volume174
Issue number9
StatePublished - 1992

Fingerprint

F Factor
Proteolysis
Proteins
DNA
DNA Replication
Plasmids
Maintenance
Escherichia coli

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Site-specific proteolysis of mini-F plasmid replication protein RepE destroys initiator function and generates an incompatibility substance. / Kline, B. C.; Sandhu, G. S.; Eckloff, B. W.; Aleff, R. A.

In: Journal of Bacteriology, Vol. 174, No. 9, 1992, p. 3004-3010.

Research output: Contribution to journalArticle

Kline, B. C. ; Sandhu, G. S. ; Eckloff, B. W. ; Aleff, R. A. / Site-specific proteolysis of mini-F plasmid replication protein RepE destroys initiator function and generates an incompatibility substance. In: Journal of Bacteriology. 1992 ; Vol. 174, No. 9. pp. 3004-3010.
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