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Identification of nuclear retention domains in the RBM20 protein
Author(s) -
Filippello Agnese,
Lorenzi Pamela,
Bergamo Elisa,
Romanelli Maria Grazia
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.07.018
Subject(s) - nuclear localization sequence , rna splicing , biology , gene , complementary dna , cloning (programming) , alternative splicing , genetics , rna binding protein , microbiology and biotechnology , computational biology , rna , messenger rna , computer science , programming language
RBM20 is a nuclear protein which regulates alternative splicing of expressed genes that have a key role in cardiac function. By cloning the human and mouse RBM20 cDNA, producing expressing vectors for truncated proteins, and comparing their sub‐cellular distribution in transfected cells, we have identified the sequences necessary for RBM20 full nuclear retention. The region overlaps an RNA binding motif and a serine–arginine domain. The sequence is conserved in many species but belongs only to RBM20 orthologs. The RMB20 tissue specificity, together with the properties of its nuclear localization determinant, demonstrates a specific evolutionary selection of post‐transcriptional regulation factors.