Detailed Information on Publication Record
2020
Recognition of RNA Polymerase II C-terminal domain by RPRD2
LINHARTOVÁ, Kateřina, Jakub MACOŠEK, Veronika JANŠTOVÁ, Eliška ŠMIŘÁKOVÁ, Karel KUBÍČEK et. al.Basic information
Original name
Recognition of RNA Polymerase II C-terminal domain by RPRD2
Authors
LINHARTOVÁ, Kateřina (203 Czech Republic, belonging to the institution), Jakub MACOŠEK (203 Czech Republic, belonging to the institution), Veronika JANŠTOVÁ (203 Czech Republic), Eliška ŠMIŘÁKOVÁ (203 Czech Republic, belonging to the institution), Karel KUBÍČEK (203 Czech Republic) and Richard ŠTEFL (203 Czech Republic, belonging to the institution)
Edition
CEITEC PhD Conference, 2020
Other information
Language
English
Type of outcome
Konferenční abstrakt
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
RIV identification code
RIV/00216224:14740/20:00118409
Organization unit
Central European Institute of Technology
Keywords in English
RNA Polymerase II C-terminal domain; RPRD2
Tags
Změněno: 17/3/2021 14:47, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
The largest subunit of human RNA Polymerase II contains highly flexible C-terminal domain (CTD) that is composed of 52 heptapeptide repeats (first half of repeats with consensus sequence YSPTSPS and second half largely degenerated in sequence). Several CTDs canonical and non-canonical residues can be subjects of post-translational modifications. Tyrosine, threonine and serine residues undergo dynamic phosphorylation/dephosphorylation resulting in specific phosphorylation patterns throughout different stages of transcription cycle. These phosphorylation patterns are recognized by various transcription and processing factors during the transcription cycle. Therefore, CTD plays an important role in the regulation of transcription and coupling of transcription to post-transcriptional processes such as mRNA processing. In this study, we show that human transcription factor, RPRD2, recognizes specifically pSer2 or pThr4 phosphorylated forms of CTD via its CTD-interacting domain (CID) in a similar way to its yeast homologue, Rtt103. The interaction of RPRD2 CID with pSer2 phosphorylated CTD is further enhanced by additional phosphorylation on pSer7. To provide mechanistic details of the interaction between RPRD2 CID and pSer2,7 CTD, the solution structure was obtained using NMR spectroscopy. pSer 2 and pTh4 phosphomarks occur mainly during the late elongation and termination. RPRD2s preference for these two phosphomarks suggests possible involvement of RPRD2 in transcription termination.
Links
LQ1601, research and development project |
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