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. 2004 Feb 27;315(1):10-5.
doi: 10.1016/j.bbrc.2004.01.018.

The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer

Akira Nakamura  1 , Hirofumi Komori, Gengo Kobayashi, Akiko Kita, Chieko Wada, Kunio Miki
Affiliations

The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer

Akira Nakamura et al. Biochem Biophys Res Commun. .

Abstract

The initiator protein RepE of the mini-F plasmid in Escherichia coli plays an essential role in DNA replication, which is regulated by the molecular chaperone-dependent oligomeric state (monomer or dimer). Crosslinking, ultracentrifugation, and gel filtration analyses showed that the solely expressed N-terminal domain (residues 1-144 or 1-152) exists in the dimeric state as in the wild-type RepE protein. This result indicates that the N-terminal domain functions as a dimerization domain of RepE and might be important for the interaction with the molecular chaperones. The N-terminal domain dimer has been crystallized in order to obtain structural insight into the regulation of the monomer/dimer conversion of RepE.

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