Identification of the methylation preference region in heterogeneous nuclear ribonucleoprotein K by protein arginine methyltransferase 1 and its implication in regulating nuclear/cytoplasmic distribution.
Biochem Biophys Res Commun
; 404(3): 865-9, 2011 Jan 21.
Article
em En
| MEDLINE
| ID: mdl-21184736
ABSTRACT
Protein arginine methylation plays crucial roles in numerous cellular processes. Heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a multi-functional protein participating in a variety of cellular functions including transcription and RNA processing. HnRNP K is methylated at multiple sites in the glycine- and arginine-rich (RGG) motif. Using various RGG domain deletion mutants of hnRNP K as substrates, here we show by direct methylation assay that protein arginine methyltransferase 1 (PRMT1) methylated preferentially in a.a. 280-307 of the RGG motif. Kinetic analysis revealed that deletion of a.a. 280-307, but not a.a. 308-327, significantly inhibited rate of methylation. Importantly, nuclear localization of hnRNP K was significantly impaired in mutant hnRNP K lacking the PRMT1 methylation region or upon pharmacological inhibition of methylation. Together our results identify preferred PRMT1 methylation sequences of hnRNP K by direct methylation assay and implicate a role of arginine methylation in regulating intracellular distribution of hnRNP K.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Arginina
/
Proteína-Arginina N-Metiltransferases
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Proteínas Repressoras
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Núcleo Celular
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Citoplasma
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Ribonucleoproteínas Nucleares Heterogêneas Grupo K
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Taiwan