Structure of the C-terminal domain of the clock protein KaiA in complex with a KaiC-derived peptide: Implications for KaiC regulation

被引:81
作者
Vakonakis, I [1 ]
LiWang, AC [1 ]
机构
[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
关键词
D O I
10.1073/pnas.0403037101
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Circadian clocks are widespread endogenous mechanisms that control the temporal pattern of diverse biological processes, including gene transcription. KaiA is the positive element of the cyanobacterial clock because KaiA overexpression elevates transcription levels of clock components. Recently, we showed that the structure of KaiA is that of a domain-swapped homodimer. The N-terminal domain is a pseudo-receiver; thus, it is likely to be involved in signal transduction in the clock-resetting pathway. The C-terminal domain of KaiA is structurally novel and enhances the KaiC autokinase activity directly. Here, we report the NMR structure of the C-terminal domain of KaiA (ThKaiA180C) in complex with a KaiC-derived peptide from the cyanobacterium Thermosynechococcus elongatus BP-1. The protein-peptide interface is revealed to be different from a model that was proposed earlier, is stabilized by a combination of hydrophobic and electrostatic interactions, and includes many residues known to produce a circadian-period phenotype upon substitution. Although the structure of the monomeric subunit of ThKaiA180C is largely unchanged upon peptide binding, the intersubunit dimerization angle changes. It is proposed that modulation of the C-terminal KaiA domain dimerization angle regulates KaiA-KaiC interactions.
引用
收藏
页码:10925 / 10930
页数:6
相关论文
共 34 条
[1]  
BUNNING E, 1973, PHYSL CLOCK CIRCADIO
[2]  
CHRISTOPHER JA, 1999, SPOCK STRUCTURAL PRO
[3]   Protein backbone angle restraints from searching a database for chemical shift and sequence homology [J].
Cornilescu, G ;
Delaglio, F ;
Bax, A .
JOURNAL OF BIOMOLECULAR NMR, 1999, 13 (03) :289-302
[4]  
Dunlap J.C., 2003, CHRONOBIOLOGY BIOL T
[5]   Molecular bases for circadian clocks [J].
Dunlap, JC .
CELL, 1999, 96 (02) :271-290
[6]   Origin and evolution of circadian clock genes in prokaryotes [J].
Dvornyk, V ;
Vinogradova, O ;
Nevo, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (05) :2495-2500
[7]   Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC [J].
Garces, RG ;
Wu, N ;
Gillon, W ;
Pai, EF .
EMBO JOURNAL, 2004, 23 (08) :1688-1698
[8]   4 HELIX BUNDLE DIVERSITY IN GLOBULAR-PROTEINS [J].
HARRIS, NL ;
PRESNELL, SR ;
COHEN, FE .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 236 (05) :1356-1368
[9]   Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC [J].
Hayashi, F ;
Ito, H ;
Fujita, M ;
Iwase, R ;
Uzumaki, T ;
Ishiura, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 316 (01) :195-202
[10]   ATP-induced hexameric ring structure of the cyanobacterial circadian clock protein KaiC [J].
Hayashi, F ;
Suzuki, H ;
Iwase, R ;
Uzumaki, T ;
Miyake, A ;
Shen, JR ;
Imada, K ;
Furukawa, Y ;
Yonekura, K ;
Namba, K ;
Ishiura, M .
GENES TO CELLS, 2003, 8 (03) :287-296