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Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis

C Wang1, K Chua, W Seghezzi

  • 1Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.pende014@mc.duke.edu

Genes & Development
|May 29, 1998
PubMed

Insights

Researchers identified the human SAP 155 protein, crucial for spliceosome assembly. This protein is phosphorylated during splicing catalysis, revealing a novel regulatory mechanism in gene expression.

Area of Science:

  • Molecular Biology
  • RNA Splicing
  • Protein Phosphorylation

Background:

  • The spliceosome is a complex molecular machine responsible for RNA splicing.
  • SAP 155 is a component of the U2 small nuclear ribonucleoprotein particle (snRNP).
  • SAP 155's position suggests a role in spliceosome catalysis.

Purpose of the Study:

  • To isolate the cDNA encoding human SAP 155.
  • To identify homologous proteins in other organisms.
  • To investigate the phosphorylation status of SAP 155 during splicing.

Main Methods:

  • cDNA isolation and sequencing.
  • Homology searches using bioinformatics tools.
  • Analysis of protein phosphorylation during in vitro splicing assays.

Main Results:

  • Human SAP 155 cDNA was isolated and characterized.
  • A highly conserved homolog of SAP 155 was identified in Saccharomyces cerevisiae.
  • SAP 155 undergoes phosphorylation during or immediately after the first catalytic step of splicing.

Conclusions:

  • SAP 155 is a conserved splicing factor with a potential link to protein phosphatase 2A (PP2A).
  • The phosphorylation of SAP 155 is tightly regulated by splicing catalysis.
  • This represents the first identified instance of protein modification linked to spliceosome catalytic activity.

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