spe-10 encodes a DHHC-CRD zinc-finger membrane protein required for endoplasmic reticulum/Golgi membrane morphogenesis during Caenorhabditis elegans spermatogenesis
| Autor: | Elizabeth J. Gleason, Tim L. Kroft, Steven W. L'Hernault, Wesley C. Lindsey, Andrew Singson |
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| Rok vydání: | 2005 |
| Předmět: |
Male
Mutant Molecular Sequence Data Mutation Missense Golgi Apparatus Investigations Protein lipidation Endoplasmic Reticulum Animals Genetically Modified Genetics Morphogenesis Animals Amino Acid Sequence Cloning Molecular Caenorhabditis elegans Caenorhabditis elegans Proteins Spermatogenesis Integral membrane protein Zinc finger Organelles biology Base Sequence Sequence Homology Amino Acid Endoplasmic reticulum Cell Membrane Wild type Membrane Proteins Zinc Fingers biology.organism_classification Spermatids Phenotype Biochemistry Membrane protein Immunoglobulin G Rabbits |
| Zdroj: | Genetics. 172(1) |
| ISSN: | 0016-6731 |
| Popis: | C. elegans spermatogenesis employs lysosome-related fibrous body–membranous organelles (FB–MOs) for transport of many cellular components. Previous work showed that spe-10 mutants contain FB–MOs that prematurely disassemble, resulting in defective transport of FB components into developing spermatids. Consequently, spe-10 spermatids are smaller than wild type and contain defective FB–MO derivatives. In this article, we show that spe-10 encodes a four-pass integral membrane protein that has a DHHC–CRD zinc-finger motif. The DHHC–CRD motif is found in a large, diverse family of proteins that have been implicated in palmitoyl transfer during protein lipidation. Seven spe-10 mutants were analyzed, including missense, nonsense, and deletion mutants. An antiserum to SPE-10 showed significant colocalization with a known marker for the FB–MOs during wild-type spermatogenesis. In contrast, the spe-10(ok1149) deletion mutant lacked detectable SPE-10 staining; this mutant lacks a spe-10 promoter and most coding sequence. The spe-10(eb64) missense mutation, which changes a conserved residue within the DHHC–CRD domain in all homologues, behaves as a null mutant. These results suggest that wild-type SPE-10 is required for the MO to properly deliver the FB to the C. elegans spermatid and the DHHC–CRD domain is essential for this function. |
| Databáze: | OpenAIRE |
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