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Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis.


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.

SUBMITTER: Wang C 

PROVIDER: S-EPMC316838 | biostudies-literature | 1998 May

REPOSITORIES: biostudies-literature

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Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis.

Wang C C   Chua K K   Seghezzi W W   Lees E E   Gozani O O   Reed R R  

Genes & development 19980501 10


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 phosph  ...[more]

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