Atomic-scale origins of slowness in the cyanobacterial circadian clock

Autor:	Masato Osako, Shinji Saito, Jun Abe, Shuji Akiyama, Eiki Yamashita, Toshifumi Mori, Takao Kondo, Takuya B. Hiyama, Atsushi Mukaiyama, Julie Wolanin, Se-Young Son
Rok vydání:	2015
Předmět:	Multidisciplinary biology ATPase Circadian clock chemistry.chemical_compound Biochemistry chemistry ATP hydrolysis Transcription (biology) KaiC biology.protein KaiA Biophysics Transferase Adenosine triphosphate
Zdroj:	Science. 349:312-316
ISSN:	1095-9203 0036-8075
DOI:	10.1126/science.1261040
Popis:	Biochemical basis of a 24-hour clock Circadian clocks keep organisms in synch with such daily cycles as illumination, activity, and food availability. The circadian clock in cyanobacteria has the necessary 24-hour period despite its three component proteins having biochemical activities that occur on a much faster time scale. Abe et al. focused on the cyanobacterial clock component KaiC, an adenosine triphosphatase (ATPase) that can autophosphorylate and autodephosphorylate. The slow ATPase activity of KaiC, which is linked to a peptide isomerisation, provided the slow kinetics that set the speed of the 24-hour clock. Chang et al. found that another clock component, KaiB, also has slow changes in its protein conformation that help to set the oscillation period of the clock and its signaling output. Science , this issue pp. 312 and 324
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::4875ce10be1d8cf11295b22c7bb8282b https://doi.org/10.1126/science.1261040 Zobrazit plný text záznamu Plný text ve formátu PDF