Identification of the structural gene for a myosin heavy-chain in Caenorhabditis elegans

1977 ◽  
Vol 114 (1) ◽  
pp. 133-140 ◽  
Author(s):  
A.R. Macleod ◽  
R.H. Waterston ◽  
R.M. Fishpool ◽  
S. Brenner
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Structural Gene ◽  
Heavy Chain

scholarly journals A screen for genetic loci required for body-wall muscle development during embryogenesis in Caenorhabditis elegans.

Genetics ◽  
1994 ◽  
Vol 137 (2) ◽  
pp. 483-498
Author(s):  
J Ahnn ◽  
A Fire
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Muscle Cell ◽  
Heavy Chain ◽  
Body Wall ◽  
Muscle Development ◽  
Contractile Function ◽  
The Body ◽  
Body Wall Muscle ◽  
Genetic Loci

Abstract We have used available chromosomal deficiencies to screen for genetic loci whose zygotic expression is required for formation of body-wall muscle cells during embryogenesis in Caenorhabditis elegans. To test for muscle cell differentiation we have assayed for both contractile function and the expression of muscle-specific structural proteins. Monoclonal antibodies directed against two myosin heavy chain isoforms, the products of the unc-54 and myo-3 genes, were used to detect body-wall muscle differentiation. We have screened 77 deficiencies, covering approximately 72% of the genome. Deficiency homozygotes in most cases stain with antibodies to the body-wall muscle myosins and in many cases muscle contractile function is observed. We have identified two regions showing distinct defects in myosin heavy chain gene expression. Embryos homozygous for deficiencies removing the left tip of chromosome V fail to accumulate the myo-3 and unc-54 products, but express antigens characteristic of hypodermal, pharyngeal and neural development. Embryos lacking a large region on chromosome III accumulate the unc-54 product but not the myo-3 product. We conclude that there exist only a small number of loci whose zygotic expression is uniquely required for adoption of a muscle cell fate.

Sequence analysis of mutations that affect the synthesis, assembly and enzymatic activity of the unc-54 myosin heavy chain of Caenorhabditis elegans

1985 ◽  
Vol 183 (4) ◽  
pp. 543-551 ◽  
Author(s):  
Nick J. Dibb ◽  
Daniel M. Brown ◽  
Jonathan Karn ◽  
Donald G. Moerman ◽  
Suzanne L. Bolten ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Sequence Analysis ◽  
Enzymatic Activity ◽  
Myosin Heavy Chain ◽  
Heavy Chain

Sequence analysis of the complete Caenorhabditis elegans myosin heavy chain gene family

1989 ◽  
Vol 205 (3) ◽  
pp. 603-613 ◽  
Author(s):  
Nick J. Dibb ◽  
Ichiro N. Maruyama ◽  
Michael Krause ◽  
Jonathan Karn
Keyword(s):  
Caenorhabditis Elegans ◽  
Sequence Analysis ◽  
Gene Family ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Chain Gene ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene

Mutations in the unc-54 myosin heavy chain gene of caenorhabditis elegans that alter contractility but not muscle structure

Cell ◽  
1982 ◽  
Vol 29 (3) ◽  
pp. 773-781 ◽  
Author(s):  
Donald G. Moerman ◽  
Santiago Plurad ◽  
Robert H. Waterston ◽  
David L. Baillie
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Chain Gene ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene ◽  
Muscle Structure

scholarly journals Caenorhabditis elegans Unc-45 Is a Component of Muscle Thick Filaments and Colocalizes with Myosin Heavy Chain B, but Not Myosin Heavy Chain a

2000 ◽  
Vol 148 (2) ◽  
pp. 375-384 ◽  
Author(s):  
Wanyuan Ao ◽  
Dave Pilgrim
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Body Wall ◽  
Thick Filament ◽  
The Body ◽  
Temperature Sensitive ◽  
Filament Assembly ◽  
Thick Filaments ◽  
Body Wall Muscles

In the nematode Caenorhabditis elegans, animals mutant in the gene encoding the protein product of the unc-45 gene (UNC-45) have disorganized muscle thick filaments in body wall muscles. Although UNC-45 contains tetratricopeptide repeats (TPR) as well as limited similarity to fungal proteins, no biochemical role has yet been found. UNC-45 reporters are expressed exclusively in muscle cells, and a functional reporter fusion is localized in the body wall muscles in a pattern identical to thick filament A-bands. UNC-45 colocalizes with myosin heavy chain (MHC) B in wild-type worms as well as in temperature-sensitive (ts) unc-45 mutants, but not in a mutant in which MHC B is absent. Surprisingly, UNC-45 localization is also not seen in MHC B mutants, in which the level of MHC A is increased, resulting in near-normal muscle thick filament structure. Thus, filament assembly can be independent of UNC-45. UNC-45 shows a localization pattern identical to and dependent on MHC B and a function that appears to be MHC B–dependent. We propose that UNC-45 is a peripheral component of muscle thick filaments due to its localization with MHC B. The role of UNC-45 in thick filament assembly seems restricted to a cofactor for assembly or stabilization of MHC B.

Molecular analysis of the unc-54 myosin heavy-chain gene of Caenorhabditis elegans

Nature ◽  
1981 ◽  
Vol 291 (5814) ◽  
pp. 386-390 ◽  
Author(s):  
Alexander R. MacLeod ◽  
Jonathan Karn ◽  
Sydney Brenner
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Molecular Analysis ◽  
Heavy Chain ◽  
Chain Gene ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene
Sign in / Sign up

Export Citation Format

Share Document