NDLI: Analysis of a Gene Encoding Rpn10 of the Fission Yeast Proteasome Reveals That the Polyubiquitin-binding Site of This Subunit Is Essential When Rpn12/Mts3 Activity Is Compromised

Content Provider	Journal of Biological Chemistry (JBC)
Author	Wilkinson, Caroline R. M. Ferrell, Katherine Penney, Mary Wallace, Mairi Dubiel, Wolfgang Gordon, Colin
Abstract	Substrates are targeted for proteolysis by the ubiquitin pathway by the addition of a polyubiquitin chain before being degraded by the 26 S proteasome. Previously, a subunit of the proteasome, S5a, was identified that was able to bind to polyubiquitinin vitro and thus proposed to act as a substrate recognition component. Deletion of the correspondingSaccharomyces cerevisiae gene, MCB1/RPN10, rendered cells viable indicating that other proteasomal polyubiquitin receptors must exist. In this study, we describepus1 + , the fission yeast homologue of RPN10. This gene is also not required for cell viability; however, the Δpus1 mutant is synthetically lethal with mutations in other proteasomal component-encoding genes, namely mts3, pad1, and mts4 (RPN12,RPN11, and RPN1). Overexpression ofpus1 + is able to rescue mts3–1 at 32 °C but overexpression of a cDNA encoding a version of Pus1 that does not bind to polyubiquitin cannot and leads to greatly reduced viability when used to rescue the mts3–1Δpus1 double mutant. The Mts3 protein was unable to bind to polyubiquitin in vitro, but the Pus1 and Mts3 proteins were found to bind to one another in vitro, which taken together with the genetic data suggests that they are also closely associated in vivo.
Related Links	http://www.jbc.org/content/275/20/15182.abstract
Ending Page	15192
Starting Page	15182
Page Count	11
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	20
Volume Number	275
DOI	10.1074/jbc.275.20.15182
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2000-05-19
Access Restriction	Open
Subject Keyword	Polymerase chain reaction (PCR) Glutathione S-transferase (GST) Polyacrylamide gel electrophoresis (PAGE) Temperature-sensitive (ts) PROTEIN SYNTHESIS POST-TRANSLATION MODIFICATION AND DEGRADATION
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The pad1 + Gene Encodes a Subunit of the 26 S Proteasome in Fission Yeast

Identification of a Yeast Transcription Factor IID Subunit, TSG2/TAF48

Cell Cycle- and Cln2p-Cdc28p-dependent Phosphorylation of the Yeast Ste20p Protein Kinase

Rpg1, the Saccharomyces cerevisiae Homologue of the Largest Subunit of Mammalian Translation Initiation Factor 3, Is Required for Translational Activity

Subunit IV of Cytochrome bc 1 Complex from Rhodobacter sphaeroides LOCALIZATION OF REGIONS ESSENTIAL FOR INTERACTION WITH THE THREE-SUBUNIT CORE COMPLEX

Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12

A HECT Domain E3 Enzyme Assembles Novel Polyubiquitin Chains

Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12*

Interaction of Translation Initiation Factor eIF4G with eIF4A in the Yeast Saccharomyces cerevisiae

Analysis of a Gene Encoding Rpn10 of the Fission Yeast Proteasome Reveals That the Polyubiquitin-binding Site of This Subunit Is Essential When Rpn12/Mts3 Activity Is Compromised

Similar Documents

The pad1 + Gene Encodes a Subunit of the 26 S Proteasome in Fission Yeast

Identification of a Yeast Transcription Factor IID Subunit, TSG2/TAF48

Cell Cycle- and Cln2p-Cdc28p-dependent Phosphorylation of the Yeast Ste20p Protein Kinase

Rpg1, the Saccharomyces cerevisiae Homologue of the Largest Subunit of Mammalian Translation Initiation Factor 3, Is Required for Translational Activity

Subunit IV of Cytochrome bc 1 Complex from Rhodobacter sphaeroides LOCALIZATION OF REGIONS ESSENTIAL FOR INTERACTION WITH THE THREE-SUBUNIT CORE COMPLEX

Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12

A HECT Domain E3 Enzyme Assembles Novel Polyubiquitin Chains

Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12*

Interaction of Translation Initiation Factor eIF4G with eIF4A in the Yeast Saccharomyces cerevisiae

Analysis of a Gene Encoding Rpn10 of the Fission Yeast Proteasome Reveals That the Polyubiquitin-binding Site of This Subunit Is Essential When Rpn12/Mts3 Activity Is Compromised