Psr1 phosphatase regulates pre-mRNA splicing through spliceosomal B complex factor Snu66.

Amjadudheen Varikkapulakkal, Balashankar R Pillai, Shravan Kumar Mishra
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Abstract

Regulated precursor messenger RNA (pre-mRNA) splicing modulates gene expression and promotes alternative splicing. The process is regulated by modifications of spliceosomal proteins and small nuclear RNAs (snRNAs). Here, we show that the protein phosphatase Psr1, known for its plasma membrane localisation and function in general stress response in Saccharomyces cerevisiae, also plays a regulatory role in pre-mRNA splicing. Independently of its presence at the plasma membrane, Psr1 binds and dephosphorylates the core splicing factor Snu66. The enzyme is not an integral component of the spliceosome. Psr1 deletion in yeast, or tethering of its catalytic mutant to Snu66, results in splicing defects of introns with non-canonical 5' splice sites (ss). While the Psr1 binding site on Snu66 is distinct from the Hub1 interaction domains (HIND), Hub1 displaces Psr1 from Snu66. Thus, Psr1 phosphatase plays a regulatory role in pre-mRNA splicing by modulating Snu66 functions.

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Psr1 磷酸酶通过剪接体 B 复合因子 Snu66 调节前 mRNA 的剪接。
受调控的前体信使 RNA(pre-mRNA)剪接可调节基因表达并促进替代剪接。这一过程受剪接体蛋白和小核 RNA(snRNA)的调节。在这里,我们发现蛋白磷酸酶 Psr1 也在前 mRNA 剪接过程中发挥调控作用。Psr1 与其在质膜上的存在无关,它能结合核心剪接因子 Snu66 并使其去磷酸化。该酶不是剪接体的组成部分。在酵母中缺失 Psr1 或将其催化突变体与 Snu66 连接,会导致具有非典型 5'剪接位点(ss)的内含子出现剪接缺陷。虽然 Snu66 上的 Psr1 结合位点与 Hub1 相互作用结构域(HIND)不同,但 Hub1 会将 Psr1 从 Snu66 上置换下来。因此,Psr1 磷酸酶通过调节 Snu66 的功能,在前 mRNA 剪接过程中发挥调控作用。
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