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1. Identification and characterization of new molecular partners for the protein arginine methyltransferase 6 (PRMT6).

Author

Alessandra Lo Sardo, Sandro Altamura, Silvia Pegoraro, Elisa Maurizio, Riccardo Sgarra, and Guidalberto Manfioletti

Subjects
Medicine, Science
Abstract

PRMT6 is a protein arginine methyltransferase that has been implicated in transcriptional regulation, DNA repair, and human immunodeficiency virus pathogenesis. Only few substrates of this enzyme are known and therefore its cellular role is not well understood. To identify in an unbiased manner substrates and potential regulators of PRMT6 we have used a yeast two-hybrid approach. We identified 36 new putative partners for PRMT6 and we validated the interaction in vivo for 7 of them. In addition, using invitro methylation assay we identified 4 new substrates for PRMT6, extending the involvement of this enzyme to other cellular processes beyond its well-established role in gene expression regulation. Holistic approaches create molecular connections that allow to test functional hypotheses. The assembly of PRMT6 protein network allowed us to formulate functional hypotheses which led to the discovery of new molecular partners for the architectural transcription factor HMGA1a, a known substrate for PRMT6, and to provide evidences for a modulatory role of HMGA1a on the methyltransferase activity of PRMT6.

Published
2013
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3. Identification and characterization of new molecular partners for the protein arginine methyltransferase 6 (PRMT6)

Author

Sandro Altamura, Silvia Pegoraro, Guidalberto Manfioletti, Alessandra Lo Sardo, Elisa Maurizio, Riccardo Sgarra, LO SARDO, Alessandra, Altamura, Sandro, Pegoraro, Silvia, Maurizio, Elisa, Sgarra, Riccardo, and Manfioletti, Guidalberto

Subjects
Proteomics, Protein-Arginine N-Methyltransferases, Methyltransferase, yeast two-hybrid, lcsh:Medicine, Computational biology, Biology, Biochemistry, Models, Biological, Chromatography, Affinity, Protein–protein interaction, Substrate Specificity, Enzyme Regulation, Transferases, Two-Hybrid System Techniques, Molecular Cell Biology, Protein Interaction Mapping, Transcriptional regulation, Signaling in Cellular Processes, Humans, Protein Interaction Domains and Motifs, HMGA1a Protein, Nuclear protein, HMGA, Protein Interactions, lcsh:Science, Transcription factor, Regulation of gene expression, Genetics, Multidisciplinary, Enzyme Classes, lcsh:R, Proteins, Nuclear Proteins, Reproducibility of Results, Methylation, Protein arginine methylation, Enzymes, Regulatory Proteins, DNA methylation, lcsh:Q, Transcriptional Signaling, Research Article, Signal Transduction, Protein Binding
Abstract

PRMT6 is a protein arginine methyltransferase that has been implicated in transcriptional regulation, DNA repair, and human immunodeficiency virus pathogenesis. Only few substrates of this enzyme are known and therefore its cellular role is not well understood. To identify in an unbiased manner substrates and potential regulators of PRMT6 we have used a yeast two-hybrid approach. We identified 36 new putative partners for PRMT6 and we validated the interaction in vivo for 7 of them. In addition, using in vitro methylation assay we identified 4 new substrates for PRMT6, extending the involvement of this enzyme to other cellular processes beyond its well-established role in gene expression regulation. Holistic approaches create molecular connections that allow to test functional hypotheses. The assembly of PRMT6 protein network allowed us to formulate functional hypotheses which led to the discovery of new molecular partners for the architectural transcription factor HMGA1a, a known substrate for PRMT6, and to provide evidences for a modulatory role of HMGA1a on the methyltransferase activity of PRMT6.

Published
2013

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