SR proteins: a conserved family of pre-mRNA splicing factors

• Published in: Genes & development Vol. 6; no. 5; pp. 837 - 847
• Main Authors: ZAHLER, A. M, LANE, W. S, STOLK, J. A, ROTH, M. B
• Format: Journal Article
• Language: English
• Published: Cold Spring Harbor, NY Cold Spring Harbor Laboratory 01.05.1992
• Subjects: Amino Acid Sequence; Animals; Biological and medical sciences; Blotting, Western; Cattle; Fundamental and applied biological sciences. Psychology; HeLa Cells; Humans; Mice; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Nuclear Proteins - chemistry; Nuclear Proteins - isolation & purification; Nuclear Proteins - metabolism; Phosphoproteins - chemistry; Phosphoproteins - isolation & purification; Phosphoproteins - metabolism; RNA Precursors - metabolism; RNA Splicing; RNA, Messenger - metabolism; Transcription. Transcription factor. Splicing. Rna processing; Human; Molecular processing; Purification; Bovine; Splicing; Nucleotide sequence; RNA binding protein; Homology; Hela cell line; Vertebrata; Mammalia; Messenger RNA; Complementary DNA; Multigene family; Artiodactyla; Molecular cloning; Ungulata
• ISSN: 0890-9369; 1549-5477
• DOI: 10.1101/gad.6.5.837

We demonstrate that four different proteins from calf thymus are able to restore splicing in the same splicing-deficient extract using several different pre-mRNA substrates. These proteins are members of a conserved family of proteins recognized by a monoclonal antibody that binds to active sites of RNA polymerase II transcription. We purified this family of nuclear phosphoproteins to apparent homogeneity by two salt precipitations. The family, called SR proteins for their serine- and arginine-rich carboxy-terminal domains, consists of at least five different proteins with molecular masses of 20, 30, 40, 55, and 75 kD. Microsequencing revealed that they are related but not identical. In four of the family members a repeated protein sequence that encompasses an RNA recognition motif was observed. We discuss the potential role of this highly conserved, functionally related set of proteins in pre-mRNA splicing.