Recognition of RNA Polymerase II C-terminal domain by RPRD2

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00118409" target="_blank" >RIV/00216224:14740/20:00118409 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.ceitec.eu/abstract-book-final-docx-pdf/f36324" target="_blank" >https://www.ceitec.eu/abstract-book-final-docx-pdf/f36324</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Recognition of RNA Polymerase II C-terminal domain by RPRD2

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Recognition of RNA Polymerase II C-terminal domain by RPRD2

Popis výsledku anglicky

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.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů