Interaction of protein phosphatase type 1 with a splicing factor

FEBS Letters

Patton, James G.¹  Hartshorne, David J.³  Erdödi, Ferenc²  Hirano, Katsuya³ 

[1] Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235, USA;Department of Medical Chemistry, University Medical School of Debrecen, Debrecen H-4026, Hungary;Muscle Biology Group, Shantz Building, University of Arizona, Tucson, AZ 85721, USA

关键词: Protein phosphatase type 1;    Two-hybrid system;    Human splicing factor PSF;   

DOI  :  10.1016/0014-5793(96)00577-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A gizzard cDNA library was screened by the two-hybrid hybtem using as bait the S isoform of the catalytic subunit of protein phosphatase 1 (PP1δ) Among the proteins identified was a fragment of the polypyrimidine tract-binding protein-associated splicing factor (PSF) and for 242 residues was 97.1% identical to the human isoforms. Binding of PSF and PP1δ was confirmed by inhibition of phosphatase activity and by an overlay technique. The PP1δ binding site was contained in the N-terminal 82 residues of the PSF fragment. PSF may therefore act as a PPl target molecule in the spliceosome.

【 授权许可】

Unknown