Arun, Mahesha and Imran K., Khana and Mamta, Verma and Sharad , Awasthia and Arumugam , Rajavelu (2020) SET7/9 interacts and methylates the ribosomal protein, eL42 and regulates protein synthesis. (BBA) - Molecular Cell Research, 1867 (2). ISSN 0167-4889

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Abstract

Methylation of proteins is emerging to be an important regulator of protein function. SET7/9, a protein lysine methyltransferase, catalyses methylation of several proteins involved in diverse biological processes. SET7/9- mediated methylation often regulates the stability, sub-cellular localization and protein-protein interactions of its substrate proteins. Here, we aimed to identify novel biological processes regulated by SET7/9 by identifying new interaction partners. For this we used yeast two-hybrid screening and identified the large subunit ribosomal protein, eL42 as a potential interactor of SET7/9. We confirmed the SET7/9-eL42 interaction by co-immunoprecipitation and GST pulldown studies. The N-terminal MORN domain of SET7/9 is essential for its interaction with eL42. Importantly, we identified that SET7/9 methylates eL42 at three different lysines - Lys53, Lys80 and Lys100 through site-directed mutagenesis. By puromycin incorporation assay, we find that SET7/9- mediated methylation of eL42 affects global translation. This study identifies a new role of the functionally versatile SET7/9 lysine methyltransferase in the regulation of global protein synthesis.

Item Type:	Article
Uncontrolled Keywords:	SETD7 RPL36A Lysine methylation Translation Protein-protein interaction
Subjects:	Mass Spectrometry And Proteomic Core Facility
Depositing User:	Central Library RGCB
Date Deposited:	04 Aug 2020 09:22
Last Modified:	04 Aug 2020 09:22
URI:	http://rgcb.sciencecentral.in/id/eprint/980

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