Role of RNA Polymerase II Carboxy-terminal Domain in Coordinating Transcription with RNA Processing

McCracken, Susan; Rosonina, Emanuel; Fong, Nova; Sikes, Martha L.; Beyer, Ann L.; O’Hare, Kevin; Shuman, Stewart; Bentley, David L.

doi:10.1101/sqb.1998.63.301

Cited by 38 publications

(39 citation statements)

References 59 publications

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“…Capping of mRNA occurs shortly after initiation of transcription (Coppola et al, 1983) and is mediated by interaction of the capping enzyme with the phosphorylated form of the RNAP II CTD (McCracken et al, 1998). Remarkably, mammalian capping enzyme binds synthetic CTD peptides containing phosphoserine at either position 2 or 5, but only Ser-5 phosphorylation stimulates guanylyltransferase activity (Ho and Shuman, 1999).…”

Section: Distinct Ctd Kinase Speci®cities and Functionsmentioning

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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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: Distinct Ctd Kinase Speci®cities and Functionsmentioning

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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“…Ceg1p has been previously shown to interact biochemically with serine-5-phosphorylated-CTD of Rpb1p McCracken et al 1997McCracken et al , 1998Yue et al 1997). Such an interaction is essential for recruitment of Ceg1p.…”

Section: ) In Comparison To the Wild-type (Ysb242) Equivalent (Rementioning

confidence: 99%

“…In budding yeast, both Ceg1p and Abd1p (RNA methyltransferase) bind directly to the phosphorylated CTD McCracken et al 1997McCracken et al , 1998Yue et al 1997). However, Cet1p does not interact directly with CTD.…”

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confidence: 99%

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A Novel Role for Cet1p mRNA 5′-Triphosphatase in Promoter Proximal Accumulation of RNA Polymerase II in Saccharomyces cerevisiase

et al. 2014

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Yeast mRNA 59-triphosphatase, Cet1p, recognizes phosphorylated-RNA polymerase II as a component of capping machinery via Ceg1p for cotranscriptional formation of mRNA cap structure that recruits cap-binding complex (CBC) and protects mRNA from exonucleases. Here, we show that the accumulation of RNA polymerase II at the promoter proximal site of ADH1 is significantly enhanced in the absence of Cet1p. Similar results are also found at other genes. Cet1p is recruited to the 59 end of the coding sequence, and its absence impairs mRNA capping, and hence CBC recruitment. However, such an impaired recruitment of CBC does not enhance promoter proximal accumulation of RNA polymerase II. Thus, Cet1p specifically lowers the accumulation of RNA polymerase II at the promoter proximal site independently of mRNA cap structure or CBC. Further, we show that Cet1p's N-terminal domain, which is not involved in mRNA capping, decreases promoter proximal accumulation of RNA polymerase II. An accumulation of RNA polymerase II at the promoter proximal site in the absence of Cet1p's N-terminal domain is correlated with reduced transcription. Collectively, our results demonstrate a novel role of Cet1p in regulation of promoter proximal accumulation of RNA polymerase II independently of mRNA capping activity, and hence transcription in vivo.

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“…15 This coupling of premRNA splicing and Pol II transcription brings another layer of regulation. [16][17][18][19][20] The C-terminal domain of Pol ll is necessary for proper pre-mRNA processing [21][22][23][24] and there are several lines of evidence indicating Pol II elongation rate affects splice site choice. [25][26][27][28][29] The fact that most introns are removed co-transcriptionally means splicing occurs while pre-mRNA is close to chromatin, which may further influence splicing decisions.…”

Section: Introductionmentioning

confidence: 99%

CRE promoter sites modulate alternative splicing via p300-mediated histone acetylation

2014

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Role of RNA Polymerase II Carboxy-terminal Domain in Coordinating Transcription with RNA Processing

Cited by 38 publications

References 59 publications

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

A Novel Role for Cet1p mRNA 5′-Triphosphatase in Promoter Proximal Accumulation of RNA Polymerase II in Saccharomyces cerevisiase

CRE promoter sites modulate alternative splicing via p300-mediated histone acetylation

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