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Serine-7 of the RNA polymerase II CTD is specifically required for snRNA gene expression (2007)

S. Egloff ; D. O'Reilly ; R. D. Chapman ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 318(5857): 1777-9. doi: 10.1126/science.1145989.

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Publication Date: 2007-12-15

Description: RNA polymerase II (Pol II) transcribes genes that encode proteins and noncoding small nuclear RNAs (snRNAs). The carboxyl-terminal repeat domain (CTD) of the largest subunit of mammalian RNA Pol II, comprising tandem repeats of the heptapeptide consensus Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7, is required for expression of both gene types. We show that mutation of serine-7 to alanine causes a specific defect in snRNA gene expression. We also present evidence that phosphorylation of serine-7 facilitates interaction with the snRNA gene-specific Integrator complex. These findings assign a biological function to this amino acid and highlight a gene type-specific requirement for a residue within the CTD heptapeptide, supporting the existence of a CTD code.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2263945/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2263945/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Egloff, Sylvain -- O'Reilly, Dawn -- Chapman, Rob D -- Taylor, Alice -- Tanzhaus, Katrin -- Pitts, Laura -- Eick, Dirk -- Murphy, Shona -- 072107/Wellcome Trust/United Kingdom -- 081312/Wellcome Trust/United Kingdom -- G0400653/Medical Research Council/United Kingdom -- G0400653(71330)/Medical Research Council/United Kingdom -- G9826944/Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1777-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079403" target="_blank"〉PubMed〈/a〉

Keywords: Alanine ; Amino Acid Sequence ; Cell Line ; Consensus Sequence ; *Gene Expression Regulation ; Heterogeneous-Nuclear Ribonucleoproteins/genetics ; Humans ; Mutation ; Oligopeptides/chemistry/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Protein Subunits/genetics/metabolism ; RNA Polymerase II/chemistry/genetics/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Messenger/genetics/metabolism ; RNA, Small Nuclear/*genetics ; Serine/*metabolism ; Templates, Genetic ; *Transcription, Genetic

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP (2013)

Muniz, L., Egloff, S., Kiss, T.

Oxford University Press

In: Nucleic Acids Research

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Publication Date: 2013-04-23

Description: Through controlling the nuclear level of active positive transcription elongation factor b (P-TEFb), the 7SK small nuclear RNA (snRNA) functions as a key regulator of RNA polymerase II transcription. Together with hexamethylene bisacetamide-inducible proteins 1/2 (HEXIM1/2), the 7SK snRNA sequesters P-TEFb into transcriptionally inactive ribonucleoprotein (RNP). In response to transcriptional stimulation, the 7SK/HEXIM/P-TEFb RNP releases P-TEFb to promote polymerase II-mediated messenger RNA synthesis. Besides transiently associating with HEXIM1/2 and P-TEFb, the 7SK snRNA stably interacts with the La-related protein 7 (Larp7) and the methylphosphate capping enzyme (MePCE). In this study, we used in vivo RNA–protein interaction assays to determine the sequence and structural elements of human 7SK snRNA directing assembly of the 7SK/MePCE/Larp7 core snRNP. MePCE interacts with the short 5'-terminal G1-U4/U106-G111 helix-tail motif and Larp7 binds to the 3'-terminal hairpin and the following U-rich tail of 7SK. The overall RNA structure and some particular nucleotides provide the information for specific binding of MePCE and Larp7. We also demonstrate that binding of Larp7 to 7SK is a prerequisite for in vivo recruitment of P-TEFb, indicating that besides providing stability for 7SK, Larp7 directly participates in P-TEFb regulation. Our results provide further explanation for the frequently observed link between Larp7 mutations and cancer development.

Print ISSN: 0305-1048

Electronic ISSN: 1362-4962

Topics: Biology