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Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis

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 (...

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Bibliographic Details
Published in:Genes & development 1998-05, Vol.12 (10), p.1409-1414
Main Authors: Wang, C, Chua, K, Seghezzi, W, Lees, E, Gozani, O, Reed, R
Format: Article
Language:English
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Summary: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.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.12.10.1409