Genetics. Published Articles Ahead of Print: April 28, 2006, Copyright © 2006
doi:10.1534/genetics.106.057976


A more recent version of this article appeared on July 1, 2006.


REGULAR RESEARCH PAPERS

A genetic suppressor of two dominant temperature sensitive (DTS) lethal proteasome mutants of Drosophila melanogaster is itself a mutated proteasome subunit gene

1 Syracuse University
2 Albion College

* To whom correspondence should be addressed. E-mail: jbelote{at}syr.edu.

Submitted on March 7, 2006
Revised on April 3, 2006
Accepted on 25 April 2006


Abstract

Two dominant temperature sensitive (DTS) lethal mutants of Drosophila melanogaster are Pros261 and Pros{beta}21, previously known as DTS5 and DTS7. Heterozygotes for either mutant die as pupae when raised at 29°, but are normally viable and fertile at 25°. Previous studies have identified these as missense mutations in the genes encoding the {beta}6 and {beta}2 subunits of the 20S proteasome, respectively. In an effort to isolate additional proteasome-related mutants a screen for dominant suppressors of Pros261 was carried out, resulting in the identification of Pros25SuDTS (originally called Su(DTS)), a missense mutation in the gene encoding the 20S proteasome {alpha}2 subunit. Pros25SuDTS acts in a dominant manner to rescue both Pros261 and Pros{beta}21 from their DTS lethal phenotypes. Using an in vivo protein degradation assay it was shown that this suppression occurs by counteracting the dominant-negative effect of the DTS mutant on proteasome activity. Pros25SuDTS is a recessive polyphasic lethal at ambient temperatures. The effects of these mutants on larval neuroblast mitosis were also examined. While Pros{beta}21 shows a modest increase in the number of defective mitotic figures, there were no defects seen with the other two mutants, other than slightly reduced mitotic indices.

Key Words: proteasome, suppressor




This article has been cited by other articles:


Home page
GeneticsHome page
J. L. Seigle, A. M. Celotto, and M. J. Palladino
Degradation of Functional Triose Phosphate Isomerase Protein Underlies sugarkill Pathology
Genetics, June 1, 2008; 179(2): 855 - 862.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
I. P. Nezis, A. Simonsen, A. P. Sagona, K. Finley, S. Gaumer, D. Contamine, T. E. Rusten, H. Stenmark, and A. Brech
Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain
J. Cell Biol., March 24, 2008; 180(6): 1065 - 1071.
[Abstract] [Full Text] [PDF]