Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing

Hau Ren Chen, Twee Y. Tsao, Chun Hong Chen, Wei Yü Tsai, Lu-Shiun Her, Milton Ming Tao Hsu, Soo Chen Cheng

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

The SNT309 gene was identified via a mutation that causes lethality of cells in combination with a prp19 mutation. We showed previously that Snt309p is a component of the Prp19p-associated complex and that Snt309p, like Prp19p, is associated with the spliceo-some immediately after or concomitantly with dissociation of U4 from the spliceosome. We show here that extracts prepared from the SNT309-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.

Original languageEnglish
Pages (from-to)5406-5411
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number10
DOIs
Publication statusPublished - 1999 May 11

Fingerprint

RNA Precursors
Spliceosomes
Mutation
Complex Mixtures
Affinity Chromatography
Genes

All Science Journal Classification (ASJC) codes

  • General

Cite this

@article{8c27f0ec540a4ecbb455b55981f0be3b,
title = "Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing",
abstract = "The SNT309 gene was identified via a mutation that causes lethality of cells in combination with a prp19 mutation. We showed previously that Snt309p is a component of the Prp19p-associated complex and that Snt309p, like Prp19p, is associated with the spliceo-some immediately after or concomitantly with dissociation of U4 from the spliceosome. We show here that extracts prepared from the SNT309-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.",
author = "Chen, {Hau Ren} and Tsao, {Twee Y.} and Chen, {Chun Hong} and Tsai, {Wei Y{\"u}} and Lu-Shiun Her and Hsu, {Milton Ming Tao} and Cheng, {Soo Chen}",
year = "1999",
month = "5",
day = "11",
doi = "10.1073/pnas.96.10.5406",
language = "English",
volume = "96",
pages = "5406--5411",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "10",

}

Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing. / Chen, Hau Ren; Tsao, Twee Y.; Chen, Chun Hong; Tsai, Wei Yü; Her, Lu-Shiun; Hsu, Milton Ming Tao; Cheng, Soo Chen.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 10, 11.05.1999, p. 5406-5411.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Snt309p modulates interactions of Prp19p with its associated components to stabilize the Prp19p-associated complex essential for pre-mRNA splicing

AU - Chen, Hau Ren

AU - Tsao, Twee Y.

AU - Chen, Chun Hong

AU - Tsai, Wei Yü

AU - Her, Lu-Shiun

AU - Hsu, Milton Ming Tao

AU - Cheng, Soo Chen

PY - 1999/5/11

Y1 - 1999/5/11

N2 - The SNT309 gene was identified via a mutation that causes lethality of cells in combination with a prp19 mutation. We showed previously that Snt309p is a component of the Prp19p-associated complex and that Snt309p, like Prp19p, is associated with the spliceo-some immediately after or concomitantly with dissociation of U4 from the spliceosome. We show here that extracts prepared from the SNT309-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.

AB - The SNT309 gene was identified via a mutation that causes lethality of cells in combination with a prp19 mutation. We showed previously that Snt309p is a component of the Prp19p-associated complex and that Snt309p, like Prp19p, is associated with the spliceo-some immediately after or concomitantly with dissociation of U4 from the spliceosome. We show here that extracts prepared from the SNT309-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.

UR - http://www.scopus.com/inward/record.url?scp=0033545859&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033545859&partnerID=8YFLogxK

U2 - 10.1073/pnas.96.10.5406

DO - 10.1073/pnas.96.10.5406

M3 - Article

VL - 96

SP - 5406

EP - 5411

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 10

ER -