期刊
NUCLEIC ACIDS RESEARCH
卷 39, 期 10, 页码 4180-4191出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq1203
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资金
- National Institutes of Health
- Michigan Agricultural Experiment Station
- Oxford University Press
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.
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