Identification of nuclear retention domains in the RBM20 protein

Abstract

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.

Keywords: Alternative splicing; BSA; Bp; DCM; GAPDH; GFP; NLS; NRS; Nuclear localization; PCR; PTB; RBM20; RBP; RNA binding protein; RRM; RT-PCR; Ribonucleoprotein; SR; base-pair(s); bovine serum albumin; cDNA; complementary DNA; dilatedcardiomyopathy; glyceraldehydes-3-phosphate dehydrogenase; green fluorescent protein; heterogenous nuclear ribonucleoproteins; hnRNP; nuclear localization signals; nuclear retention signal; polymerase chainreaction; polypyrimidine tract-binding protein; reverse transcription polymerase chain reaction; ribonucleic acid recognition motif; serine/arginine-rich protein.