Open AccessSnt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing
Author(s) -
Hau Ren Chen,
Twee Tsao,
Chun Hong Chen,
Wei Yü Tsai,
Lu Shiun Her,
Milton Ming Tao Hsu,
Soo Chen Cheng
Publication year - 1999
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.96.10.5406
Subject(s) - rna splicing , messenger rna , alternative splicing , computational biology , biology , precursor mrna , microbiology and biotechnology , chemistry , genetics , rna , gene
TheSNT309 gene was identified via a mutation that causes lethality of cells in combination with aprp19 mutation. We showed previously that Snt309p is a component of the Prp19p-associated complex and that Snt309p, like Prp19p, is associated with the spliceosome immediately after or concomitantly with dissociation of U4 from the spliceosome. We show here that extracts prepared from theSNT309 -deleted strain (ΔSNT309) were defective in splicing but could be complemented by addition of the purified Prp19p-associated complex. Isolation of the Prp19p-associated complex from ΔSNT309 extracts indicated that the complex was destabilized in the absence of Snt309p and dissociated on affinity chromatography, suggesting a role of Snt309p in stabilization of the Prp19p-associated complex. Addition of the affinity-purified Prp19p–Snt309p binary complex to ΔSNT309 extracts could reconstitute the Prp19p-associated complex. Genetic analysis further suggests that Snt309p plays a role in modulating interactions of Prp19p with other associated components to facilitate formation of the Prp19p-associated complex. A model for how Snt309p modulates such interactions is proposed.