Analysis of a gene required for membrane fusion during nematode spermiogenesis

Persistent Link:
http://hdl.handle.net/10150/282106
Title:
Analysis of a gene required for membrane fusion during nematode spermiogenesis
Author:
Achanzar, William Edward, 1967-
Issue Date:
1996
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
C. elegans spermatids contain large vesicles called membranous organelles (MOs) that fuse with the plasma membrane during maturation to spermatozoa. This fusion is essential since mutations in the gene fer-1 block MO-plasma membrane fusion and result in abnormal spermatozoa. To determine the function of the fer-1 gene product during sperm maturation, I have cloned and sequenced the gene and several cDNAs. fer-1 is approximately 8.6kb in length and encodes a 6.3kb sperm-specific transcript. In situ hybridization experiments have shown fer-1 expression is limited to the primary spermatocytes, the cells in which the MOs are formed. fer-1 is predicted to encode a 235kD basic integral membrane protein (FER-1) that is highly charged and rich in lysine and glutamic acid. Database searches revealed FER-1 is similar to several predicted human proteins of unknown function. Mutations have been identified for four of the eleven fer-1 alleles, all of which cause amino acid changes in this predicted protein. FER-1 contains no recognizable functional motifs other than a single transmembrane domain at the C-terminus, a feature common to viral membrane fusion proteins. Antibodies raised against FER-1 and used for immunolocalization and western blot experiments did not yield reliable results. The work presented in this dissertation gives some evidence for my hypothesis that FER-1 is a membrane fusion protein, although the membrane fusion defect observed could be an indirect result of fer-1 mutations.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Biology, Molecular.; Biology, Cell.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Molecular and Cellular Biology
Degree Grantor:
University of Arizona
Advisor:
Ward, Samuel

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleAnalysis of a gene required for membrane fusion during nematode spermiogenesisen_US
dc.creatorAchanzar, William Edward, 1967-en_US
dc.contributor.authorAchanzar, William Edward, 1967-en_US
dc.date.issued1996en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractC. elegans spermatids contain large vesicles called membranous organelles (MOs) that fuse with the plasma membrane during maturation to spermatozoa. This fusion is essential since mutations in the gene fer-1 block MO-plasma membrane fusion and result in abnormal spermatozoa. To determine the function of the fer-1 gene product during sperm maturation, I have cloned and sequenced the gene and several cDNAs. fer-1 is approximately 8.6kb in length and encodes a 6.3kb sperm-specific transcript. In situ hybridization experiments have shown fer-1 expression is limited to the primary spermatocytes, the cells in which the MOs are formed. fer-1 is predicted to encode a 235kD basic integral membrane protein (FER-1) that is highly charged and rich in lysine and glutamic acid. Database searches revealed FER-1 is similar to several predicted human proteins of unknown function. Mutations have been identified for four of the eleven fer-1 alleles, all of which cause amino acid changes in this predicted protein. FER-1 contains no recognizable functional motifs other than a single transmembrane domain at the C-terminus, a feature common to viral membrane fusion proteins. Antibodies raised against FER-1 and used for immunolocalization and western blot experiments did not yield reliable results. The work presented in this dissertation gives some evidence for my hypothesis that FER-1 is a membrane fusion protein, although the membrane fusion defect observed could be an indirect result of fer-1 mutations.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectBiology, Molecular.en_US
dc.subjectBiology, Cell.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorWard, Samuelen_US
dc.identifier.proquest9706141en_US
dc.identifier.bibrecord.b34180333en_US
All Items in UA Campus Repository are protected by copyright, with all rights reserved, unless otherwise indicated.