p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F09%3A00333651" target="_blank" >RIV/68378050:_____/09:00333651 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization

Popis výsledku v původním jazyce

RECQL4 belongs to the conserved RecQ family of DNA helicases playing important roles in the maintenance of genome stability. Although genetic alterations in RECQL4 gene are reported to be associated with three autosomal recessive disorders, the molecularrole of RECQL4 is still poorly understood. We show that RECQL4 specifically interacts with histone acetyltransferase p300 (p300 HAT) in vivo and in vitro and that p300 acetylates one or more lysine residues of RECQL4. We also report that these residueslie within a short motif of 30 aa essential for the nuclear localization of RECQL4. Acetylation of RECQL4 by p300 in vivo leads to a significant shift of a proportion of RECQL4 protein from the nucleus to the cytoplasm. This is a result of RECQL4 inability to be imported into the nucleus. Our results are the first evidence of post-translational modification of RECQL4 and suggest that acetylation of RECQL4 by p300 regulates trafficking of RECQL4 between the nucleus and the cytoplasm.

Název v anglickém jazyce

p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization

Popis výsledku anglicky

RECQL4 belongs to the conserved RecQ family of DNA helicases playing important roles in the maintenance of genome stability. Although genetic alterations in RECQL4 gene are reported to be associated with three autosomal recessive disorders, the molecularrole of RECQL4 is still poorly understood. We show that RECQL4 specifically interacts with histone acetyltransferase p300 (p300 HAT) in vivo and in vitro and that p300 acetylates one or more lysine residues of RECQL4. We also report that these residueslie within a short motif of 30 aa essential for the nuclear localization of RECQL4. Acetylation of RECQL4 by p300 in vivo leads to a significant shift of a proportion of RECQL4 protein from the nucleus to the cytoplasm. This is a result of RECQL4 inability to be imported into the nucleus. Our results are the first evidence of post-translational modification of RECQL4 and suggest that acetylation of RECQL4 by p300 regulates trafficking of RECQL4 between the nucleus and the cytoplasm.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název periodika

Journal of Cell Science

ISSN

0021-9533

e-ISSN

—

Svazek periodika

122

Číslo periodika v rámci svazku

Pt 8

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

—

Kód UT WoS článku

000264777700023

EID výsledku v databázi Scopus

—