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Title: Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome

Abstract

Yeast Prp19 has been shown to involve in pre-mRNA splicing and DNA repair as well as being an ubiquitin ligase. Mammalian homologue of yeast Prp19 also plays on similar functional activities in cells. In the present study, we isolated mouse SUG1 (mSUG1) as binding partner of mouse Prp19 (mPrp19) by the yeast two-hybrid system. We confirmed the interaction of mPrp9 with mSUG1 by GST pull-down assay and co-immunoprecipitation assay. The N-terminus of mPrp19 including U-box domain was associated with the C-terminus of mSUG1. Although, mSUG1 is a regulatory subunit of 26S proteasome, mPrp19 was not degraded in the proteasome-dependent pathway. Interestingly, GFP-mPrp19 fusion protein was co-localized with mSUG1 protein in cytoplasm as the formation of the speckle-like structures in the presence of a proteasome inhibitor MG132. In addition, the activity of proteasome was increased in cells transfected with mPrp19. Taken together, these results suggest that mPrp19 involves the regulation of protein turnover and may transport its substrates to 26S proteasome through mSUG1 protein.

Authors:
 [1];  [2];  [3];  [3];  [3];  [4]
  1. Department of Biology, Kyung Hee University, Seoul 130-701 (Korea, Republic of)
  2. (Korea, Republic of)
  3. R and D Center, AmorePacific Corporation, Yongin-si, Gyeonggi-do 446-729 (Korea, Republic of)
  4. Department of Biology, Kyung Hee University, Seoul 130-701 (Korea, Republic of) and Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul 130-701 (Korea, Republic of). E-mail: shkim@khu.ac.kr
Publication Date:
OSTI Identifier:
20991314
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 356; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2007.02.134; PII: S0006-291X(07)00407-X; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CYTOPLASM; DNA REPAIR; GENE REGULATION; HYBRID SYSTEMS; LIGASES; MICE; SPLICING; SUBSTRATES; YEASTS

Citation Formats

Sihn, Choong-Ryoul, Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul 130-701, Cho, Si Young, Lee, Jeong Ho, Lee, Tae Ryong, and Kim, Sang Hoon. Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.02.134.
Sihn, Choong-Ryoul, Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul 130-701, Cho, Si Young, Lee, Jeong Ho, Lee, Tae Ryong, & Kim, Sang Hoon. Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome. United States. doi:10.1016/j.bbrc.2007.02.134.
Sihn, Choong-Ryoul, Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul 130-701, Cho, Si Young, Lee, Jeong Ho, Lee, Tae Ryong, and Kim, Sang Hoon. Fri . "Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome". United States. doi:10.1016/j.bbrc.2007.02.134.
@article{osti_20991314,
title = {Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome},
author = {Sihn, Choong-Ryoul and Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul 130-701 and Cho, Si Young and Lee, Jeong Ho and Lee, Tae Ryong and Kim, Sang Hoon},
abstractNote = {Yeast Prp19 has been shown to involve in pre-mRNA splicing and DNA repair as well as being an ubiquitin ligase. Mammalian homologue of yeast Prp19 also plays on similar functional activities in cells. In the present study, we isolated mouse SUG1 (mSUG1) as binding partner of mouse Prp19 (mPrp19) by the yeast two-hybrid system. We confirmed the interaction of mPrp9 with mSUG1 by GST pull-down assay and co-immunoprecipitation assay. The N-terminus of mPrp19 including U-box domain was associated with the C-terminus of mSUG1. Although, mSUG1 is a regulatory subunit of 26S proteasome, mPrp19 was not degraded in the proteasome-dependent pathway. Interestingly, GFP-mPrp19 fusion protein was co-localized with mSUG1 protein in cytoplasm as the formation of the speckle-like structures in the presence of a proteasome inhibitor MG132. In addition, the activity of proteasome was increased in cells transfected with mPrp19. Taken together, these results suggest that mPrp19 involves the regulation of protein turnover and may transport its substrates to 26S proteasome through mSUG1 protein.},
doi = {10.1016/j.bbrc.2007.02.134},
journal = {Biochemical and Biophysical Research Communications},
number = 1,
volume = 356,
place = {United States},
year = {Fri Apr 27 00:00:00 EDT 2007},
month = {Fri Apr 27 00:00:00 EDT 2007}
}