Intricate Protein-Protein Interactions in the Cyanobacterial Circadian Clock

被引：18
作者：
Egli, Martin [1 ,2 ]
机构：
[1] Vanderbilt Univ, Sch Med, Dept Biochem, Nashville, TN 37232 USA
[2] Vanderbilt Univ, Sch Med, Struct Biol Ctr, Nashville, TN 37232 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2014年 / 289卷 / 31期
基金：
美国国家卫生研究院;
关键词：
KAIB-KAIC COMPLEX; C-TERMINAL DOMAIN; SYNECHOCOCCUS-ELONGATUS; CRYSTAL-STRUCTURE; ATPASE ACTIVITY; IN-VITRO; PHOSPHORYLATION; OSCILLATOR; DYNAMICS; RHYTHM;
D O I：
10.1074/jbc.R114.579607
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The cyanobacterial circadian clock consists of a post-translational oscillator (PTO) and a PTO-dependent transcription-translation feedback loop (TTFL). The PTO can be reconstituted in vitro with the KaiA, KaiB, and KaiC proteins, enabling detailed biochemical and biophysical investigations. Both the CI and the CII halves of the KaiC hexamer harbor ATPases, but only the C-terminal CII ring exhibits kinase and phospho-transferase activities. KaiA stimulates the kinase and KaiB associates with KaiC during the dephosphorylation phase and sequesters KaiA. Recent research has led to conflicting models of the KaiB-KaiC interaction, precluding a clear understanding of KaiB function and KaiABC clock mechanism.
引用
收藏
页码：21267 / 21275
页数：9
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