The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer |
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Authors: | Nakamura Akira Komori Hirofumi Kobayashi Gengo Kita Akiko Wada Chieko Miki Kunio |
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Affiliation: | Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan. |
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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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Keywords: | Replication initiator Dimerization domain RepE Mini-F plasmid DnaK chaperone Crystallization |
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