Circadian Formation of Clock Protein Complexes by KaiA, KaiB, KaiC, and SasA in Cyanobacteria
Physical interactions among clock-related proteins KaiA, KaiB, KaiC, and SasA are proposed to be important for circadian function in the cyanobacterium Synechococcus elongatus PCC 7942. Here we show that the Kai proteins and SasA form heteromultimeric protein complexes dynamically in a circadian fas...
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Veröffentlicht in: | The Journal of biological chemistry 2003-01, Vol.278 (4), p.2388-2395 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Physical interactions among clock-related proteins KaiA, KaiB, KaiC, and SasA are proposed to be important for circadian function
in the cyanobacterium Synechococcus elongatus PCC 7942. Here we show that the Kai proteins and SasA form heteromultimeric protein complexes dynamically in a circadian
fashion. KaiC forms protein complexes of â¼350 and 400â600 kDa during the subjective day and night, respectively, and serves
as a core of the circadian protein complexes. This change in the size of the KaiC-containing complex is accompanied by nighttime-specific
interaction of KaiA and KaiB with KaiC. In various arrhythmic mutants that lack each functional Kai protein or SasA, circadian
rhythms in formation of the clock protein complex are abolished, and the size of the protein complexes is dramatically affected.
Thus, circadian-regulated formation of the clock protein complexes is probably a critical process in the generation of circadian
rhythm in cyanobacteria. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M208899200 |