Quick Search:

uzh logo
Browse by:
bullet
bullet
bullet
bullet

Zurich Open Repository and Archive 

Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-17968

Dietschy, T; Shevelev, I; Pena-Diaz, J; Hühn, D; Kuenzle, S; Mak, R; Miah, M F; Hess, D; Fey, M; Hottiger, M O; Janscak, P; Stagljar, I (2009). p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization. Journal of Cell Science, 122(Pt. 8):1258-1267.

[img]
Preview
PDF
1MB

Abstract

RECQL4 belongs to the conserved RecQ family of DNA helicases, members of which play important roles in the maintenance of genome stability in all organisms that have been examined. Although genetic alterations in the RECQL4 gene are reported to be associated with three autosomal recessive disorders (Rothmund-Thomson, RAPADILINO and Baller-Gerold syndromes), the molecular role of RECQL4 still remains poorly understood. Here, we show that RECQL4 specifically interacts with the histone acetyltransferase p300 (also known as p300 HAT), both in vivo and in vitro, and that p300 acetylates one or more of the lysine residues at positions 376, 380, 382, 385 and 386 of RECQL4. Furthermore, we report that these five lysine residues lie within a short motif of 30 amino acids that is essential for the nuclear localization of RECQL4. Remarkably, the 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 accumulation of the acetylated RECQL4 is a result of its inability to be imported into the nucleus. Our results provide the first evidence of a post-translational modification of the RECQL4 protein, and suggest that acetylation of RECQL4 by p300 regulates the trafficking of RECQL4 between the nucleus and the cytoplasm.

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Veterinary Biochemistry and Molecular Biology
04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
DDC:570 Life sciences; biology
Language:English
Date:15 April 2009
Deposited On:26 Mar 2009 10:13
Last Modified:27 Nov 2013 16:55
Publisher:Company of Biologists
ISSN:0021-9533
Additional Information:Free full text article
Publisher DOI:10.1242/jcs.037747
PubMed ID:19299466
Citations:Web of Science®. Times Cited: 17
Google Scholar™
Scopus®. Citation Count: 11

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page