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Recognition of RNA Polymerase II C-terminal domain by RPRD2

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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

Alternative languages

  • Result language

    angličtina

  • Original language name

    Recognition of RNA Polymerase II C-terminal domain by RPRD2

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

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

  • Continuities

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

Others

  • Publication year

    2020

  • Confidentiality

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