RRC ID 3203
著者 Fujikawa N, Kurumizaka H, Yamazoe M, Hiraga S, Yokoyama S.
タイトル Identification of functional domains of the Escherichia coli SeqA protein.
ジャーナル Biochem. Biophys. Res. Commun.
Abstract The Escherichia coli SeqA protein, a negative regulator of chromosomal DNA replication, prevents the overinitiation of replication within one cell cycle by binding to hemimethylated G-mA-T-C sequences in the replication origin, oriC. In addition to the hemimethylated DNA-binding activity, the SeqA protein has a self-association activity, which is also considered to be essential for its regulatory function in replication initiation. To study the functional domains responsible for the DNA-binding and self-association activities, we performed a deletion analysis of the SeqA protein and found that the N-terminal (amino acid residues 1-59) and the C-terminal (amino acid residues 71-181) regions form structurally distinct domains. The N-terminal domain, which is not involved in DNA binding, has the self-association activity. In contrast, the C-terminal domain, which lacks the self-association activity, specifically binds to the hemimethylated G-mA-T-C sequence. Therefore, two essential SeqA activities, self-association and DNA-binding, are independently performed by the structurally distinct N-terminal and C-terminal domains, respectively.
巻・号 300(3)
ページ 699-705
公開日 2003-1-1
PII S0006291X02028917
PMID 12507506
MeSH Bacterial Outer Membrane Proteins Chromatography, Gel DNA / metabolism DNA Methylation DNA Replication / physiology DNA-Binding Proteins Escherichia coli Escherichia coli Proteins Mutagenesis, Site-Directed Protein Structure, Tertiary / physiology Sequence Deletion Structure-Activity Relationship Transcription Factors / chemistry* Transcription Factors / genetics*
IF 2.466
引用数 8
原核生物(大腸菌) CV-25(DH5alpha)?