crystal structure of circadian clock protein kaia from synechococcus elongatus
In molecular biology, the
cyanobacterial clock proteins are the main circadian regulator in cyanobacteria. The cyanobacterial clock proteins comprise three proteins: KaiA, KaiB and KaiC. The kaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction.
In the complex, KaiA enhances the
phosphorylation status of kaiC. In contrast, the presence of kaiB in the complex decreases the phosphorylation status of kaiC, suggesting that kaiB acts by antagonising the interaction between kaiA and kaiC. The activity of KaiA activates kaiBC expression, while KaiC represses it. The overall fold of the KaiA monomer is that of a four- helix bundle, which forms a dimer in the known structure. KaiA functions as a [1 ] homodimer. Each monomer is composed of three functional domains: the N-terminal amplitude-amplifier domain, the central period-adjuster domain and the C-terminal clock-oscillator domain. The N-terminal domain of KaiA, from cyanobacteria, acts as a pseudo-receiver domain, but lacks the conserved aspartyl residue required for phosphotransfer in response regulators. The C-terminal domain is responsible for dimer formation, binding to KaiC, enhancing KaiC [2 ] phosphorylation and generating the circadian oscillations. The KaiA protein from [3 ] sp. (strain PCC 7120) lacks the N-terminal CheY-like domain. Anabaena
KaiB adopts an alpha-beta meander
motif and is found to be a dimer or a tetramer. [1 ] [4 ]
KaiC belongs to a larger
family of proteins; it performs autophosphorylation and acts as its own transcriptional repressor. It binds ATP. [5 ]
Also in the KiaC family is RadA/Sms, a highly conserved eubacterial protein that shares
sequence similarity with both RecA strand transferase and lon protease. The RadA/Sms family are probable ATP-dependent proteases involved in both DNA repair and degradation of proteins, peptides, glycopeptides. They are classified in as non-peptidase homologues and unassigned peptidases in MEROPS peptidase family S16 (lon protease family, clan SJ). RadA/Sms is involved in recombination and recombinational repair, most likely involving the stabilisation or processing of branched DNA molecules or blocked replication forks because of its genetic redundancy with RecG and RuvABC. [6 ]
References [ edit ]
^ a b Garces RG, Wu N, Gillon W, Pai EF (April 2004). "Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC". EMBO J. 23 (8): 1688–98. doi: 10.1038/sj.emboj.7600190. PMC 394244. PMID 15071498.
^ Williams SB, Vakonakis I, Golden SS, LiWang AC (November 2002). "Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15357–62. doi: 10.1073/pnas.232517099. PMC 137721. PMID 12438647.
^ Uzumaki T, Fujita M, Nakatsu T, Hayashi F, Shibata H, Itoh N, Kato H, Ishiura M (July 2004). "Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein". Nat. Struct. Mol. Biol. 11 (7): 623–31. doi: 10.1038/nsmb781. PMID 15170179.
^ Hitomi K, Oyama T, Han S, Arvai AS, Getzoff ED (2005). "Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm.". J Biol Chem 280 (19): 19127–35. doi: 10.1074/jbc.M411284200. PMID 15716274.
^ Pattanayek R, Wang J, Mori T, Xu Y, Johnson CH, Egli M (2004). "Visualizing a circadian clock protein: crystal structure of KaiC and functional insights.". Mol Cell 15 (3): 375–88. doi: 10.1016/j.molcel.2004.07.013. PMID 15304218.
^ Beam CE, Saveson CJ, Lovett ST (December 2002). "Role for radA/sms in recombination intermediate processing in Escherichia coli". J. Bacteriol. 184 (24): 6836–44. doi: 10.1128/jb.184.24.6836-6844.2002. PMC 135464. PMID 12446634.
This article incorporates text from the public domain Pfam and InterPro IPR011648
This article incorporates text from the public domain Pfam and InterPro IPR011649
This article incorporates text from the public domain Pfam and InterPro IPR014774