Abstract
The U2 snRNP component SAP 155 contacts pre-mRNA on both sides of the branch site early in spliceosome assembly and is therefore positioned near or at the spliceosome catalytic center. We have isolated a cDNA encoding human SAP 155 and identified its highly related Saccharomyces cerevisiae homolog (50% identity). The carboxy-terminal two-thirds of SAP 155 shows the highest conservation and is remarkably similar to the regulatory subunit A of the phosphatase PP2A. Significantly, SAP 155 is phosphorylated concomitant with or just after catalytic step one, making this the first example of a protein modification tightly regulated with splicing catalysis.
MeSH Terms
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Binding Sites
Caenorhabditis elegans/genetics
Catalysis
Consensus Sequence
DNA, Complementary/genetics
Genes, Fungal
Helminth Proteins/chemistry
Humans
Macromolecular Substances
Molecular Sequence Data
Phosphoprotein Phosphatases/chemistry
Phosphoproteins/genetics,metabolism
Phosphorylation
Protein Binding
Protein Processing, Post-Translational
RNA Precursors/metabolism
RNA Splicing/physiology
RNA Splicing Factors
Ribonucleoprotein, U2 Small Nuclear/genetics,metabolism
Saccharomyces cerevisiae/genetics
Saccharomyces cerevisiae Proteins
Schizosaccharomyces/genetics
Sequence Alignment
Sequence Homology, Amino Acid
Spliceosomes/metabolism
Chemicals
Adaptor Proteins, Signal Transducing
DNA, Complementary
Helminth Proteins
Macromolecular Substances
Phosphoproteins
RNA Precursors
RNA Splicing Factors
Ribonucleoprotein, U2 Small Nuclear
SAP155 protein, S cerevisiae
SF3B1 protein, human
Saccharomyces cerevisiae Proteins
Phosphoprotein Phosphatases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Wang C
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.pende014@mc.duke.edu
Chua K
Seghezzi W
Lees E
Gozani O
Reed R
References (23)
23 references, click to expand
-
Substrates for p34cdc2: in vivo veritas?
Cell. 1990 May 18;61(4):549-51
PMID: 2188729
-
Evidence that U5 snRNP recognizes the 3' splice site for catalytic step II in mammals.
EMBO J. 1997 Aug 1;16(15):4746-59
PMID: 9303319
-
A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription.
J Cell Biol. 1991 Nov;115(3):587-96
PMID: 1717489
-
Site-specific modification of pre-mRNA: the 2'-hydroxyl groups at the splice sites.
Science. 1992 May 15;256(5059):992-7
PMID: 1589782
-
Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing.
Nucleic Acids Res. 1992 Oct 25;20(20):5263-9
PMID: 1331983
-
Thiophosphorylation of U1-70K protein inhibits pre-mRNA splicing.
Nature. 1993 May 20;363(6426):283-6
PMID: 8387646
-
Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors.
Nucleic Acids Res. 1993 Jun 25;21(12):2815-22
PMID: 8332490
-
Correspondence between a mammalian spliceosome component and an essential yeast splicing factor.
Science. 1993 Oct 1;262(5130):105-8
PMID: 8211113
-
Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens.
J Virol. 1994 Jan;68(1):123-9
PMID: 8254721
-
A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction.
EMBO J. 1994 Jul 15;13(14):3356-67
PMID: 8045264
-
The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition.
Genes Dev. 1994 Apr 1;8(7):843-54
PMID: 7926772
-
Purification and characterization of a kinase specific for the serine- and arginine-rich pre-mRNA splicing factors.
Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10824-8
PMID: 7526381
-
Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism.
EMBO J. 1994 Dec 1;13(23):5679-88
PMID: 7988565
-
CUS1, a suppressor of cold-sensitive U2 snRNA mutations, is a novel yeast splicing factor homologous to human SAP 145.
Genes Dev. 1996 Jan 15;10(2):220-32
PMID: 8566755
-
Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A.
Genes Dev. 1996 Jan 15;10(2):233-43
PMID: 8566756
-
The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution.
EMBO J. 1996 Jan 15;15(2):265-75
PMID: 8617202
-
Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly.
Mol Cell Biol. 1996 Jul;16(7):3317-26
PMID: 8668147
-
Initial splice-site recognition and pairing during pre-mRNA splicing.
Curr Opin Genet Dev. 1996 Apr;6(2):215-20
PMID: 8722179
-
The structure and function of proteins involved in mammalian pre-mRNA splicing.
Annu Rev Biochem. 1996;65:367-409
PMID: 8811184
-
Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing.
Genes Dev. 1997 Feb 1;11(3):334-44
PMID: 9030686
-
The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that can be phosphorylated by the snRNP-associated protein kinase.
RNA. 1997 Apr;3(4):344-55
PMID: 9085842
-
Protein functions in pre-mRNA splicing.
Curr Opin Cell Biol. 1997 Jun;9(3):320-8
PMID: 9159080
-
Protein composition of mammalian spliceosomes assembled in vitro.
Proc Natl Acad Sci U S A. 1990 Oct;87(20):8031-5
PMID: 2146679