Proper expression of myosin genes in transgenic nematodes

Caenorhabditis elegans has four genes which encode skeletal myosin heavy chain isoforms. We have re‐introduced clones of two of these genes, myo‐3 and unc‐54 at low copy number into the germline of C. elegans. The resulting loci behave as functional copies of the genes by two genetic criteria: (i) t...

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Bibliographic Details
Published in:The EMBO journal 1989-11, Vol.8 (11), p.3419-3428
Main Authors: Fire, A., Waterston, R.H.
Format: Article
Language:English
Subjects:
Animals
Animals, Genetically Modified
Biological and medical sciences
Blotting, Southern
Caenorhabditis - genetics
Caenorhabditis elegans
Crosses, Genetic
Fundamental and applied biological sciences. Psychology
Gene Expression
Genes
Genetic Complementation Test
Molecular and cellular biology
Molecular genetics
Mutation
Myosins - biosynthesis
Myosins - genetics
Phenotype
Transfection
Transformation, Genetic
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Summary:Caenorhabditis elegans has four genes which encode skeletal myosin heavy chain isoforms. We have re‐introduced clones of two of these genes, myo‐3 and unc‐54 at low copy number into the germline of C. elegans. The resulting loci behave as functional copies of the genes by two genetic criteria: (i) they can result in phenotypic rescue of strains carrying inactivating myo‐3 or unc‐54 mutations, and (ii) their presence in strains with wild‐type copies of the endogenous myosin loci has genetic consequences similar to duplicating the endogenous loci. The re‐introduced genes function at a level close to that of the endogenous loci. Monoclonal antibodies specific for the different isoforms have been used to localize the expressed proteins. The re‐introduced genes express in precisely the same cell types as the endogenous genes, and the myosin products produced assemble into filament structures as in wild‐type. Unexpectedly, we have found in the course of this work that very high copy numbers of the unc‐54 gene lead to a disruption of muscle structure which may result from overexpression of the protein product.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1989.tb08506.x