TheKIN28Gene is Required both for RNA Polymerase II Mediated Transcription and Phosphorylation of the Rpb1p CTD

Valay, Jean-Gabriel; Simon, Michel; Dubois, Marie-Françoise; Bensaude, Olivier; Facca, Céline; Faye, Gérard

doi:10.1006/jmbi.1995.0316

Cited by 176 publications

(199 citation statements)

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“…There is good evidence that mammalian CDK7 and its functional counterpart Kin28 in budding yeast are the major CTD kinases in vivo (Valay et al, 1995;Rossi et al, 2001). However, the exact functional role of RNAP II CTD phosphorylation by CDK7 remains to be de®ned.…”

Section: Cdks Associated With the Rnap II Transcription Machinerymentioning

confidence: 99%

“…Thus, CDK7 kinase activity per se appears not to be limiting for cell cycle progression Adamczewski et al, 1996;Nigg, 1996). Matters were further complicated by the discovery that CTD kinase activity in budding yeast (S. cerevisiae) is provided by the TFIIH subunit Kin28 which does not possess CAK activity, while CAK functions are mediated by the kinase Cak1, which is unrelated to CDK7 (Feaver et al, 1994;Cismowski et al, 1995;Valay et al, 1995). Finally, ®ssion yeast (Schizosaccharomyces pombe), in which cell cycle regulation is considered to be evolutionary closer to metazoans than to budding yeast, was found to contain two CAKs: a complex composed of the CDK7 ortholog Mcs6 and the cyclin H-related protein Mcs2 which exhibits CAK activity as well as CTD kinase activity, and the Csk1 kinase.…”

Section: Cdks Associated With the Rnap II Transcription Machinerymentioning

confidence: 99%

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Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control

Oelgeschläger

2002

Journal Cellular Physiology

128

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The carboxyl-terminal domain (CTD) of the largest subunit of mammalian RNA polymerase II (RNAP II) consists of 52 repeats of a consensus heptapeptide and is subject to phosphorylation and dephosphorylation events during each round of transcription. RNAP II activity is regulated during the cell cycle and cell cycledependend changes in RNAP II activity correlate well with CTD phosphorylation. In addition, global changes in the CTD phosphorylation status are observed in response to mitogenic or cytostatic signals such as growth factors, mitogens and DNA-damaging agents. Several CTD kinases are members of the cyclindependent kinase (CDK) superfamily and associate with transcription initiation complexes. Other CTD kinases implicated in cell cycle regulation include the mitogen-activated protein kinases ERK-1/2 and the c-Abl tyrosine kinase. These observations suggest that reversible RNAP II CTD phosphorylation may play a key role in linking cell cycle regulatory events to coordinated changes in transcription.

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Section: Cdks Associated With the Rnap II Transcription Machinerymentioning

confidence: 99%

Section: Cdks Associated With the Rnap II Transcription Machinerymentioning

confidence: 99%

Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control

Oelgeschläger

2002

Journal Cellular Physiology

128

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“…There also exist other Cdk family members functioning in other cellular events: Ccl1 cyclin-Kin28 kinase (Cismowski et al 1995;Valay et al 1995) and Srb11 cyclin-Srb10 kinase (Liao et al 1995) are involved in the phosphorylation of the Cterminal domain of the largest subunit of RNA polymerase II. Whether these Cdks are involved in cell-cycle regulation is not yet clear, but Pho85p was shown to associate with G 1 -cyclin homologues, including Pcl1p, Pcl2p and Pcl9p (Espinoza et al 1994;Measday et al 1994Measday et al , 1997.…”

Section: Introductionmentioning

confidence: 99%

The Pho85 kinase, a member of the yeast cyclin‐ dependent kinase (Cdk) family, has a regulation mechanism different from Cdks functioning throughout the cell cycle

et al. 1999

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Background: The PHO85 gene is a negative regulator of the PHO system in the yeast Saccharomyces cerevisiae and encodes a protein kinase (Pho85p) which is highly homologous to the Cdc28 kinase (Cdc28p). Although the two kinases share a 51% identity and their functional domains are well conserved, PHO85 fails to replace CDC28. Pho85p forms complexes with G 1 -cyclin homologues, including Pcl1p, Pcl2p and Pcl9p, and is thought to be involved in the cell-cycle regulation at G 1 and the end of M. By analysing the genetic and biochemical properties of Pho85p, we studied whether the regulation of Pho85p activity is similar to other cyclin-dependent kinases (Cdks) directly involved in cell cycle regulation.

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“…The RNA polymerase II CTD plays an essential role in mRNA synthesis, and its phosphorylation is a key feature of its function (8). The first CTD kinase, Kin28p, is associated with Ccl1p, a C-type cyclin, and with a third factor, Rig2p (12,61,62). This complex, like its human counterpart the Cdk7p kinase complex (37), is a component of the general transcription factor TFIIH (44,58).…”

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confidence: 99%

The Yeast C-Type Cyclin Ctk2p Is Phosphorylated and Rapidly Degraded by the Ubiquitin-Proteasome Pathway

Hautbergue

Goguel

1999

Molecular and Cellular Biology

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The yeast CTDK-I complex has been implicated in phosphorylation of the carboxy-terminal domain of the RNA polymerase II and in transcription control. It is composed of three polypeptides: Ctk1p and Ctk2p, a cyclin-dependent kinase and a C-type cyclin subunit, respectively; and Ctk3p, a third subunit of unknown function. Cyclins are regulatory proteins whose expression is tightly controlled at the protein level. In this study, we examined the regulation of Ctk2p expression in vivo. Surprisingly, unlike what has been described for cell cycle cyclins, steady-state levels of Ctk2p are composed of two relatively abundant forms, one of them phosphorylated. We show that this phosphorylated form is extremely unstable (half-life, 5 min) and that rapid proteolysis of Ctk2p exhibits growth-related regulation. Furthermore, our data establish that similar to the case for other naturally short-lived proteins, Ctk2p degradation is mediated by the ubiquitin-proteasome pathway. This is the first demonstration that a C-type cyclin is phosphorylated and targeted to the proteasome. Strikingly, neither phosphorylation nor destruction of Ctk2p requires its associated kinase Ctk1p, a feature fundamentally different from that which has been observed for cell cycle cyclins.Cyclin-dependent protein kinases (CDKs) were first identified as central regulators of the major transitions of the eukaryotic cell division cycle. Their activity is determined by cyclin binding, by both positive and negative regulatory phosphorylation, and by polypeptide CDK inhibitors (40, 41). A single cyclin-dependent kinase subunit associates sequentially with multiple cyclin partners whose abundance fluctuates during the cell cycle (43). Indeed, one aspect of CDK regulation is triggered by the rapid destruction of their cyclin partners (23). Several studies both in yeast and in mammals have demonstrated that cyclins are selectively degraded by the ubiquitindependent proteasome pathway (9,16,53,67). Substrates are first marked for degradation by conjugation with several molecules of ubiquitin, a highly conserved 76-amino-acid-long polypeptide that is joined reversibly by a covalent linkage.

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TheKIN28Gene is Required both for RNA Polymerase II Mediated Transcription and Phosphorylation of the Rpb1p CTD

Cited by 176 publications

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Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control

Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control

The Pho85 kinase, a member of the yeast cyclin‐ dependent kinase (Cdk) family, has a regulation mechanism different from Cdks functioning throughout the cell cycle

The Yeast C-Type Cyclin Ctk2p Is Phosphorylated and Rapidly Degraded by the Ubiquitin-Proteasome Pathway

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