Journal Article

Two forms of ribosomal protein L2 of <i>Escherichia coli</i> that inhibit DnaA in DNA replication

Sundari Chodavarapu, Magdalena M. Felczak and Jon M. Kaguni

in Nucleic Acids Research

Volume 39, issue 10, pages 4180-4191
Published in print May 2011 | ISSN: 0305-1048
Published online February 2011 | e-ISSN: 1362-4962 | DOI: https://dx.doi.org/10.1093/nar/gkq1203

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We purified an inhibitor of oriC plasmid replication and determined that it is a truncated form of ribosomal protein L2 evidently lacking 59 amino acid residues from the C-terminal region encoded by rplB. We show that this truncated form of L2 or mature L2 physically interacts with the N-terminal region of DnaA to inhibit initiation from oriC by apparently interfering with DnaA oligomer formation, and the subsequent assembly of the prepriming complex on an oriC plasmid. Both forms of L2 also inhibit the unwinding of oriC by DnaA. These in vitro results raise the possibility that one or both forms of L2 modulate DnaA function in vivo to regulate the frequency of initiation.

Journal Article.  7669 words.  Illustrated.

Subjects: Chemistry ; Biochemistry ; Bioinformatics and Computational Biology ; Genetics and Genomics ; Molecular and Cell Biology

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