| Nuclear structure and chromosome segregation in Drosophila male meiosis depend on the ubiquitin ligase dTopors. | |
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MedLine Citation:
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PMID: 21900273 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In many organisms, homolog pairing and synapsis at meiotic prophase depend on interactions between chromosomes and the nuclear membrane. Male Drosophila lack synapsis, but nonetheless, their chromosomes closely associate with the nuclear periphery at prophase I. To explore the functional significance of this association, we characterize mutations in nuclear blebber (nbl), a gene required for both spermatocyte nuclear shape and meiotic chromosome transmission. We demonstrate that nbl corresponds to dtopors, the Drosophila homolog of the mammalian dual ubiquitin/small ubiquitin-related modifier (SUMO) ligase Topors. We show that mutations in dtopors cause abnormalities in lamin localizations, centriole separation, and prophase I chromatin condensation and also cause anaphase I bridges that likely result from unresolved homolog connections. Bridge formation does not require mod(mdg4) in meiosis, suggesting that bridges do not result from misregulation of the male homolog conjunction complex. At the ultrastructural level, we observe disruption of nuclear shape, an uneven perinuclear space, and excess membranous structures. We show that dTopors localizes to the nuclear lamina at prophase, and also transiently to intranuclear foci. As a role of dtopors at gypsy insulator has been reported, we also asked whether these new alleles affected expression of the gypsy-induced mutation ct(6) and found that it was unaltered in dtopors homozygotes. Our results indicate that dTopors is required for germline nuclear structure and meiotic chromosome segregation, but in contrast, is not necessary for gypsy insulator function. We suggest that dtopors plays a structural role in spermatocyte lamina that is critical for multiple aspects of meiotic chromosome transmission. |
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Authors:
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Maiko Matsui; Krishn C Sharma; Carol Cooke; Barbara T Wakimoto; Mohammad Rasool; Miranda Hayworth; Christopher A Hylton; John E Tomkiel |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-09-06 |
Journal Detail:
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Title: Genetics Volume: 189 ISSN: 1943-2631 ISO Abbreviation: Genetics Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-15 Completed Date: 2012-03-01 Revised Date: 2013-02-19 |
Medline Journal Info:
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Nlm Unique ID: 0374636 Medline TA: Genetics Country: United States |
Other Details:
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Languages: eng Pagination: 779-93 Citation Subset: IM |
Affiliation:
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Department of Biology, University of North Carolina, Greensboro, North Carolina 27402, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alleles Amino Acid Sequence Anaphase / genetics Animals Cell Nucleus / enzymology, genetics, metabolism* Centrioles / enzymology, genetics, metabolism Chromatin / genetics, metabolism Chromosome Segregation* / genetics Chromosomes, Insect / enzymology, genetics* DNA-Binding Proteins / genetics Drosophila Proteins / chemistry, genetics, metabolism* Drosophila melanogaster / cytology*, enzymology*, genetics, metabolism Epistasis, Genetic / genetics Female Humans Male Meiosis / genetics* Mice Molecular Sequence Data Mutation RNA-Binding Proteins / genetics Ubiquitin-Protein Ligases / chemistry, genetics, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM079780-01A1/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Chromatin; 0/DNA-Binding Proteins; 0/Drosophila Proteins; 0/RNA-Binding Proteins; 0/modulo protein, Drosophila; EC 6.3.2.19/Topors protein, Drosophila; EC 6.3.2.19/Ubiquitin-Protein Ligases |
| Comments/Corrections | |
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