A Universal RNA Polymerase II CTD Cycle Is Orchestrated by Complex Interplays between Kinase, Phosphatase, and Isomerase Enzymes along Genes

被引:171
作者
Bataille, Alain R. [1 ]
Jeronimo, Celia [1 ]
Jacques, Pierre-Etienne [1 ]
Laramee, Louise [1 ]
Fortin, Marie-Eve [1 ]
Forest, Audrey [1 ]
Bergeron, Maxime [1 ]
Hanes, Steven D. [2 ]
Robert, Francois [1 ,3 ]
机构
[1] Inst Rech Clin Montreal, Montreal, PQ H2W 1R7, Canada
[2] Upstate Med Univ, Syracuse, NY 13210 USA
[3] Univ Montreal, Fac Med, Dept Med, Montreal, PQ H3C 3J7, Canada
关键词
ESS1; PROLYL-ISOMERASE; CARBOXY-TERMINAL DOMAIN; PRE-MESSENGER-RNA; TRANSCRIPTION ELONGATION; TFIIH KINASE; PHOSPHORYLATION; RECRUITMENT; METHYLATION; SSU72; DEACETYLATION;
D O I
10.1016/j.molcel.2011.11.024
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Transcription by RNA polymerase II (RNAPII) is coupled to mRNA processing and chromatin modifications via the C-terminal domain (CTD) of its largest subunit, consisting of multiple repeats of the heptapeptide YSPTSPS. Pioneering studies showed that CTD serines are differentially phosphorylated along genes in a prescribed pattern during the transcription cycle. Genome-wide analyses challenged this idea, suggesting that this cycle is not uniform among different genes. Moreover, the respective role of enzymes responsible for CTD modifications remains controversial. Here, we systematically profiled the location of the RNAPII phosphoisoforms in wildtype cells and mutants for most CTD modifying enzymes. Together with results of in vitro assays, these data reveal a complex interplay between the modifying enzymes, and provide evidence that the CTD cycle is uniform across genes. We also identify Ssu72 as the Ser7 phosphatase and show that proline isomerization is a key regulator of CTD dephosphorylation at the end of genes.
引用
收藏
页码:158 / 170
页数:13
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