Advances in the study of SR protein family.
- Author:
Xiaoyun MA
1
;
Fuchu HE
Author Information
1. Beijing Institute of Radiation Medicine, Beijing 100850, China.
- Publication Type:Journal Article
- MeSH:
Alternative Splicing;
Amino Acid Motifs;
Evolution, Molecular;
Heterogeneous-Nuclear Ribonucleoproteins;
chemistry;
Humans;
Phosphorylation;
Protein Binding;
Protein Conformation;
Protein Structure, Tertiary;
Proteomics;
methods;
RNA;
chemistry;
Spliceosomes;
chemistry;
metabolism
- From:
Genomics, Proteomics & Bioinformatics
2003;1(1):2-8
- CountryChina
- Language:English
-
Abstract:
The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS domain, and also possess special biochemical and immunological features. As to the functions of SR proteins, they facilitate the recruitment of the components of splicesome via protein-protein interaction to prompt the assembly of early splicesome; while in alternative splicing, tissue-specifically expressed SR protein along with the relative ratio of SR protein and heterogeneous nuclear ribonucleoprotein (hnRNP) is composed of two main regulative mechanisms to alternative splicing. Almost all of the biochemical functions are regulated by reversible phosphorylation.
