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The Pad1+ gene encodes a subunit of the 26 S proteasome in fission yeast

M Penney1, C Wilkinson, M Wallace

  • 1MRC Human Genetics Unit Western General Hospital, Edinburgh EH4 2XU Scotland, United Kingdom.

The Journal of Biological Chemistry
|September 3, 1998
PubMed

Insights

We identified the Pad1 protein as a new subunit of the 26S proteasome in fission yeast. This discovery links Pad1 to proteasome function and methyl 2-benzimidazolecarbamate resistance in Schizosaccharomyces pombe.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The 26S proteasome is a crucial protein complex for cellular protein degradation.
  • Mutations in proteasome subunits can lead to various cellular defects, including drug resistance and temperature sensitivity.
  • Previous screens in Schizosaccharomyces pombe identified mutations in proteasome subunits Mts2, Mts3, and Mts4.

Purpose of the Study:

  • To identify novel genes involved in proteasome function using a genetic screen.
  • To characterize the function of the pad1(+) gene in fission yeast.
  • To determine if Pad1 is a component of the 26S proteasome.

Main Methods:

  • Genetic screening for methyl 2-benzimidazolecarbamate resistance (MBCR) and temperature sensitivity (ts) in Schizosaccharomyces pombe.
  • Gene sequencing to identify the mutation in the mts5-1 strain.
  • Genetic interaction studies to assess the relationship between Pad1 and known proteasome subunits.
  • Biochemical methods to confirm Pad1 as a proteasome subunit.

Main Results:

  • The mutation conferring MBCR and ts phenotypes in the mts5-1 strain was identified in the pad1(+) gene.
  • The pad1-1 mutation exhibits similar phenotypes to known 26S proteasome mutants.
  • Pad1 shows genetic interactions with proteasome subunits Mts3 and Mts4.
  • Pad1 was identified as a subunit of the 26S proteasome in fission yeast.

Conclusions:

  • Pad1 is a novel subunit of the 26S proteasome in fission yeast.
  • Pad1 plays a role in proteasome function and cellular response to methyl 2-benzimidazolecarbamate.
  • The findings provide new insights into the composition and regulation of the 26S proteasome.

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