Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1
Autore:
Kzhyshkowska, J; Schutt, H; Liss, M; Kremmer, E; Staubert, R; Wolf, H; Dobner, T;
Indirizzi:
Univ Regensburg, Inst Med Mikrobiol & Hyg, D-93053 Regensburg, Germany Univ Regensburg Regensburg Germany D-93053 , D-93053 Regensburg, Germany GSF, Inst Mol Immunol, D-81337 Munich, Germany GSF Munich Germany D-81337 SF, Inst Mol Immunol, D-81337 Munich, Germany Univ Erlangen Nurnberg, Inst Klin & Mol Virol, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Erlangen Germany D-91054 -91054 Erlangen, Germany
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 358, anno: 2001,
parte:, 2
pagine: 305 - 314
SICI:
0264-6021(20010901)358:<305:HNREIM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-BINDING PROTEINS; NUCLEOCYTOPLASMIC TRANSPORT; N-METHYLTRANSFERASE; MOLECULAR-WEIGHT; TERMINAL DOMAIN; IN-VITRO; HNRNP-U; CELLS; EXPORT; A1;
Keywords:
periodate-oxidized adenosine; S-adenosylmethionine; SH3 domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Kzhyshkowska, J Klinikum Univ Heidelberg, Klinikum Mannheim GmbH, DermatolKlin, Theodor Kutzer Ufer 1-3, D-68167 Mannheim, Germany Klinikum Univ Heidelberg Theodor Kutzer Ufer 1-3 Mannheim Germany D-68167
Citazione:
J. Kzhyshkowska et al., "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1", BIOCHEM J, 358, 2001, pp. 305-314

Abstract

The heterogeneous nuclear ribonucleoprotein (hnRNP) family includes predominantly nuclear proteins acting at different stages of mRNA metabolism. A characteristic feature of hnRNPs is to undergo post-translational asymmetricarginine methylation catalysed by different type 1 protein arginine methyltransferases (PRMTs). A novel mammalian hnRNP, E1B-AP5, recently identifiedby its interaction with adenovirus early protein E1B-55 kDa, has been proposed to have a regulatory role in adenoviral and host-cell mRNA processing/nuclear export [Gabler, Schutt, Groid, Wolf, Shenk and Dobner (1998) J. Virol. 72, 7960-7971]. Here we report that E1B-AP5 is methylated in vivo in its Arg-Gly-Gly (RGG)-box domain, known to mediate protein-RNA interactions. The activity responsible for E1B-AP5 methylation forms a complex with E1B-AP5 in vivo. The predominant mammalian arginine methyltransferase HRM1L2 (hPRMT1) did not detectably methylate endogenous E1B-AP5 despite efficiently methylating a recombinant RGG-box domain of E1B-AP5. Using yeast two-hybrid screening we identified HRMT1L1 (PRMT2) as one of the proteins interacting with E1B-AP5. By in situ immunofluorescence we demonstrated that E1B-AP5 co-localizes with the nuclear fraction of HRMT1L1. The Src homology 3 (SH3) domain of HRMT1L1 was essential for its interaction with E1B-AP5 in vivo. Wesuggest that HRMT1L1 is responsible for specific E1B-AP5 methylation in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 16:15:14