G1 cyclin-Cdk promotes cell cycle entry through localized phosphorylation of RNA polymerase II.
Science
; 374(6565): 347-351, 2021 Oct 15.
Article
en En
| MEDLINE
| ID: mdl-34648313
ABSTRACT
Cell division is thought to be initiated by cyclin-dependent kinases (Cdks) inactivating key transcriptional inhibitors. In budding yeast, the G1 cyclin Cln3-Cdk1 complex is thought to directly phosphorylate the Whi5 protein, thereby releasing the transcription factor SBF and committing cells to division. We report that Whi5 is a poor substrate of Cln3-Cdk1, which instead phosphorylates the RNA polymerase II subunit Rpb1's C-terminal domain on S5 of its heptapeptide repeats. Cln3-Cdk1 binds SBF-regulated promoters and Cln3's function can be performed by the canonical S5 kinase Ccl1-Kin28 when synthetically recruited to SBF. Thus, we propose that Cln3-Cdk1 triggers cell division by phosphorylating Rpb1 at SBF-regulated promoters to promote transcription. Our findings blur the distinction between cell cycle and transcriptional Cdks to highlight the ancient relationship between these two processes.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
ARN Polimerasa II
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División Celular
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Proteína Quinasa CDC28 de Saccharomyces cerevisiae
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Ciclinas
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Proteínas de Saccharomyces cerevisiae
Idioma:
En
Revista:
Science
Año:
2021
Tipo del documento:
Article
País de afiliación:
Estados Unidos