KUBÍČEK, Karel, Hana ČERNÁ, Peter HOLUB, Josef PASULKA, Dominika HROŠŠOVÁ, Frank LOEHR, Ctirad HOFR, Štěpánka VAŇÁČOVÁ and Richard ŠTEFL. Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1. Genes & Development. New York: Cold Spring Harbor Laboratory Press, 2012, vol. 26, No 17, p. 1891-1896. ISSN 0890-9369. doi:10.1101/gad.192781.112.
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Basic information
Original name Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1
Authors KUBÍČEK, Karel (203 Czech Republic, belonging to the institution), Hana ČERNÁ (203 Czech Republic, belonging to the institution), Peter HOLUB (203 Czech Republic, belonging to the institution), Josef PASULKA (203 Czech Republic, belonging to the institution), Dominika HROŠŠOVÁ (703 Slovakia, belonging to the institution), Frank LOEHR (276 Germany), Ctirad HOFR (203 Czech Republic, belonging to the institution), Štěpánka VAŇÁČOVÁ (203 Czech Republic, belonging to the institution) and Richard ŠTEFL (203 Czech Republic, guarantor, belonging to the institution).
Edition Genes & Development, New York, Cold Spring Harbor Laboratory Press, 2012, 0890-9369.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10610 Biophysics
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 12.444
RIV identification code RIV/00216224:14740/12:00057508
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1101/gad.192781.112
UT WoS 000308391800002
Keywords in English RNA polymerase II; CTD code; phosphorylation; proline isomerization; RNA processing and degradation; NMR spectroscopy; structure
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 7. 4. 2013 04:28.
Abstract
Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5–Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code.
Links
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
GAP205/12/0550, research and development projectName: Dynamika vzniku shelterinového komplexu
Investor: Czech Science Foundation
GAP305/10/1490, research and development projectName: Strukturní podstata ukončení transkripce nezávislé na poly(A) signálu
Investor: Czech Science Foundation
GAP305/11/1095, research and development projectName: Funkční a biochemická charakterizace proteinu Dis3L2, třetího lidského homologu hlavní kvasinkové exosomové nukleázy Dis3p
Investor: Czech Science Foundation, Functional and biochemical characterization of Dis3L2, the third mammalian homolog of the key yeast exosome nuclease Dis3p
GBP305/12/G034, research and development projectName: Centrum biologie RNA
084316/Z/07/Z, interní kód MUName: Polyadenylation and mechanisms of nuclear RNA quality control
Investor: Wellcome Trust, Polyadenylation and mechanisms of nuclear RNA quality control
1642, interní kód MUName: EMBO Young Investigator Programme (Acronym: EMBO)
Investor: EMBO (European Molecular Biology Organization), EMBO Young Investigator Programme
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