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Hydrolysis of the IciA protein, an inhibitor of DNA replication initiation, by protease Do in Escherichia coli
Author(s) -
Yoo Soon Ji,
Seol Jae Hong,
Woo Seung Kyoon,
Suh Se Won,
Hwang Deog Su,
Ha Doo Bong,
Chung Chin Ha
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81029-y
Subject(s) - seqa protein domain , escherichia coli , protease , biology , dna replication , biochemistry , dna , microbiology and biotechnology , chemistry , gene , enzyme , eukaryotic dna replication
The 33 kDa IciA protein, an inhibitor of replication initiation of the Escherichia coli chromosome, was found to be specifically cleaved to 27 kDa fragment by protease Do, the htrA gene product. The 27 kDa polypeptide could no longer interact with the oriC region, and therefore the cleavage‐site is likely to reside within the N‐terminal DNA‐binding domain of the IciA protein. In addition, protease Do was found to localize primarily to the cytoplasm although it also could bind to membranes through an ionic interaction. These results suggest that intracellular breakdown of the IciA protein by protease Do may provide a potential mechanism involving the regulation of initiation of DNA replication in Escherichia coli .