ArticleMolecular biology of the cell1996
CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p.
Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 53 citations in OpenAlex.
- De novo 2q36.3q37.1 deletion encompassingHuman genome variation · 2020Article
- The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome.Molecular biology of the cell · 2007Article
- Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import.Molecular biology of the cell · 2006Article
- Molecular sequelae of proteasome inhibition in human multiple myeloma cells.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats.The Biochemical journal · 2002Article
- HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.Molecular biology of the cell · 2001Article
- RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane.Molecular biology of the cell · 2000Article
- Rpn9 is required for efficient assembly of the yeast 26S proteasome.Molecular and cellular biology · 1999Article
- Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome.Molecular biology of the cell · 1999Article
- A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology.Molecular biology of the cell · 1998Article
- The regulatory particle of the Saccharomyces cerevisiae proteasome.Molecular and cellular biology · 1998Article
- Modulation of the intracellular stability and toxicity of diphtheria toxin through degradation by the N-end rule pathway.The EMBO journal · 1998Article
- Evidence that mating by the Saccharomyces cerevisiae gpa1Val50 mutant occurs through the default mating pathway and a suggestion of a role for ubiquitin-mediated proteolysis.Molecular biology of the cell · 1997Article
- The 26S proteasome: subunits and functions.Molecular biology reports · 1997Review
- Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.Molecular biology of the cell · 1997Article
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Authors and funding
16 authors at 8 institutions in 4 countries.
Funding
Abstract
The 26S proteasome is a large multisubunit protease complex, the largest regulatory subunit of which is a component named p112. Molecular cloning of cDNA encoding human p112 revealed a polypeptide predicted to have 953 amino acid residues and a molecular mass of 105,865. The human p112 gene was mapped to the q37.1-q37.2 region of chromosome 2. Computer analysis showed that p112 has strong similarity to the Saccharomyces cerevisiae Sen3p, which has been listed in a gene bank as a factor affecting tRNA splicing endonuclease. The SEN3 also was identified in a synthetic lethal screen with the nin1-1 mutant, a temperature-sensitive mutant of NIN1. NIN1 encodes p31, another regulatory subunit of the 26S proteasome, which is necessary for activation of Cdc28p kinase. Disruption of the SEN3 did not affect cell viability, but led to temperature-sensitive growth. The human p112 cDNA suppressed the growth defect at high temperature in a SEN3 disruptant, indicating that p112 is a functional homologue of the yeast Sen3p. Maintenance of SEN3 disruptant cells at the restrictive temperature resulted in a variety of cellular dysfunctions, including defects in proteolysis mediated by the ubiquitin pathway, in the N-end rule system, in the stress response upon cadmium exposure, and in nuclear protein transportation. The functional abnormality induced by SEN3 disruption differs considerably from various phenotypes shown by the nin1-1 mutation, suggesting that these two regulatory subunits of the 26S proteasome play distinct roles in the various processes mediated by the 26S proteasome.
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