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1型蛋白磷酸酶与一种剪接因子的相互作用。

Interaction of protein phosphatase type 1 with a splicing factor.

作者信息

Hirano K, Erdödi F, Patton J G, Hartshorne D J

机构信息

Muscle Biology Group, University of Arizona, Tucson, 85721, USA.

出版信息

FEBS Lett. 1996 Jul 1;389(2):191-4. doi: 10.1016/0014-5793(96)00577-7.

Abstract

A gizzard cDNA library was screened by the two-hybrid system using as bait the delta isoform of the catalytic subunit of protein phosphatase 1 (PP1delta). 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 PP1delta was confirmed by inhibition of phosphatase activity and by an overlay technique. The PP1delta binding site was contained in the N-terminal 82 residues of the PSF fragment. PSF may therefore act as a PP1 target molecule in the spliceosome.

摘要

利用蛋白磷酸酶1(PP1δ)催化亚基的δ同工型作为诱饵,通过双杂交系统筛选砂囊cDNA文库。鉴定出的蛋白质中有一段多嘧啶序列结合蛋白相关剪接因子(PSF)片段,其242个残基与人类同工型的同源性为97.1%。通过抑制磷酸酶活性和覆盖技术证实了PSF与PP1δ的结合。PP1δ结合位点位于PSF片段的N端82个残基中。因此,PSF可能在剪接体中作为PP1的靶分子发挥作用。

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