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PMID: 9556329 Published · ppublish English Journal Article

Depletion of a Drosophila homolog of yeast Sup35p disrupts spindle assembly, chromosome segregation, and cytokinesis during male meiosis.

Cell motility and the cytoskeleton ·Vol. 39 ·No. 4 ·1998-00-00 ·Pages 286-302

Basu J, Williams BC, Li Z, Williams EV, Goldberg ML

Abstract

In the course of a genetic screen for male-sterile mutations in Drosophila affecting chromosome segregation during the meiotic divisions in spermatocytes, we identified the mutation dsup35(63D). Examination of mutant testes showed that chromosome misbehavior was a consequence of major disruptions in meiotic spindle assembly. These perturbations included problems in aster formation, separation, and migration around the nuclear envelope; aberrations in spindle organization and integrity; and disappearance of the ana/telophase central spindle, which in turn disrupts cytokinesis. The dsup35(63D) mutation is caused by a P element insertion that affects, specifically in the testis, the expression of a gene (dsup35) encoding the Drosophila homolog of the yeast Sup35p and Xenopus eRF3 proteins. These proteins are involved in the termination of polypeptide synthesis on ribosomes, but previous studies have suggested that Sup35p and closely related proteins of the same family also interact directly with microtubules. An affinity-purified antibody directed against the product of the dsup35 gene was prepared; interestingly, this antibody specifically labels primary spermatocytes in one or two discrete foci of unknown structure within the nucleoplasm. We discuss how depletion of the dsup35 gene product in spermatocytes might lead to the global disruptions in meiotic spindle assembly seen in mutant spermatocytes.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Division/genetics Chromosomes/genetics,physiology Drosophila melanogaster/genetics,physiology Fungal Proteins/genetics Gene Deletion Humans Male Meiosis/genetics Molecular Sequence Data Mutagenesis Peptide Termination Factors/genetics Prions Saccharomyces cerevisiae/genetics Saccharomyces cerevisiae Proteins Spermatocytes/metabolism Spindle Apparatus/genetics Testis/metabolism
Chemicals
Fungal Proteins Peptide Termination Factors Prions SUP35 protein, S cerevisiae Saccharomyces cerevisiae Proteins peptide-chain-release factor 3
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Basu J
Section of Genetics and Development, Cornell University, Ithaca, New York 14853-2703, USA.
Williams B C
Li Z
Williams E V
Goldberg M L
Article Info
Journal
Cell motility and the cytoskeleton
Abbr.
Cell Motil Cytoskeleton
ISSN
0886-1544
Published
1998-00-00
Pages
286-302
Language
English
Region
United States
NLM ID
8605339
Subset
IM
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