http://www.cnr.it/ontology/cnr/individuo/prodotto/ID183654

PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity. (Articolo in rivista)

Type

Label

PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity. (Articolo in rivista) (literal)

Anno

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

Alternative label

Scebba Francesca, De Bastiani Morena, Bernacchia Giovanni, Andreucci Andrea, Galli Alvaro, Pitto Letizia (2007)
PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity.
in Plant journal (Print)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Scebba Francesca, De Bastiani Morena, Bernacchia Giovanni, Andreucci Andrea, Galli Alvaro, Pitto Letizia (literal)

Pagina inizio

Pagina fine

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

Rivista

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

Note

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

1Laboratorio di Terapia Genica e Molecolare, Istituto di Fisiologia Clinica, Area della Ricerca CNR, Italy, 2Dipartimento di Biologia ed Evoluzione, Sez. Biologia Evolutiva, Universita` di Ferrara, Ferrara, Italy, and 3Dipartimento di Scienze Botaniche, Universita` di Pisa, Pisa, Italy (literal)

Titolo

PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity. (literal)

Abstract

Plant methyl-DNA-binding proteins (MBDs), discovered by sequence homology to their animal counterparts, have not been well characterized at the physiological and functional levels. In order better to characterize the Arabidopsis AtMBD7 protein, unique in bearing three MBD domains, we used a yeast two-hybrid system to identify its partners. One of the interacting proteins we cloned is the Arabidopsis arginine methyltransferase 11 (AtPRMT11). Glutathione S-transferase pull-down and co-immunoprecipitation assays confirmed that the two proteins interact with each other and can be co-isolated. Using GFP fluorescence, we show that both AtMBD7 and AtPRMT11 are present in the nucleus. Further analyses revealed that AtPRMT11 acts as an arginine methyltransferase active on both histones and proteins of cellular extracts. The analysis of a T-DNA mutant line lacking AtPRMT11 mRNA revealed reduced levels of proteins with asymmetrically dimethylated arginines, suggesting that AtPRMT11, which is highly similar to mammalian PRMT1, is indeed a type I arginine methyltransferase. Further, AtMBD7 is a substrate for AtPRMT11, which post-translationally modifies the portion of the protein-containing C-terminal methylated DNA-binding domain. These results suggest the existence of a link between DNA methylation and arginine methylation. (literal)

Prodotto di