Recognition of RNA Polymerase II C-terminal domain by RPRD2

a 2020

Recognition of RNA Polymerase II C-terminal domain by RPRD2

LINHARTOVÁ, Kateřina, Jakub MACOŠEK, Veronika JANŠTOVÁ, Eliška ŠMIŘÁKOVÁ, Karel KUBÍČEK et. al.

Základní údaje

Originální název

Recognition of RNA Polymerase II C-terminal domain by RPRD2

Autoři

LINHARTOVÁ, Kateřina (203 Česká republika, domácí), Jakub MACOŠEK (203 Česká republika, domácí), Veronika JANŠTOVÁ (203 Česká republika), Eliška ŠMIŘÁKOVÁ (203 Česká republika, domácí), Karel KUBÍČEK (203 Česká republika) a Richard ŠTEFL (203 Česká republika, domácí)

Vydání

CEITEC PhD Conference, 2020

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/20:00118409

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

RNA Polymerase II C-terminal domain; RPRD2

Štítky

rivok

Změněno: 17. 3. 2021 14:47, Mgr. Pavla Foltynová, Ph.D.

Anotace

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.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

LINHARTOVÁ, Kateřina, Jakub MACOŠEK, Veronika JANŠTOVÁ, Eliška ŠMIŘÁKOVÁ, Karel KUBÍČEK a Richard ŠTEFL. Recognition of RNA Polymerase II C-terminal domain by RPRD2. In CEITEC PhD Conference. 2020.

@proceedings{1753038,
   author = {Linhartová, Kateřina and Macošek, Jakub and Janštová, Veronika and Šmiřáková, Eliška and Kubíček, Karel and Štefl, Richard},
   booktitle = {CEITEC PhD Conference},
   keywords = {RNA Polymerase II C-terminal domain; RPRD2},
   language = {eng},
   title = {Recognition of RNA Polymerase II C-terminal domain by RPRD2},
   url = {https://www.ceitec.eu/abstract-book-final-docx-pdf/f36324},
   year = {2020}
}

TY  - CONF
ID  - 1753038
AU  - Linhartová, Kateřina - Macošek, Jakub - Janštová, Veronika - Šmiřáková, Eliška - Kubíček, Karel - Štefl, Richard
PY  - 2020
TI  - Recognition of RNA Polymerase II C-terminal domain by RPRD2
KW  - RNA Polymerase II C-terminal domain
KW  - RPRD2
UR  - https://www.ceitec.eu/abstract-book-final-docx-pdf/f36324
N2  - 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.
ER  -

LINHARTOVÁ, Kateřina, Jakub MACOŠEK, Veronika JANŠTOVÁ, Eliška ŠMIŘÁKOVÁ, Karel KUBÍČEK a Richard ŠTEFL. Recognition of RNA Polymerase II C-terminal domain by RPRD2. In \textit{CEITEC PhD Conference}. 2020.

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