Worm Breeder's Gazette 11(2): 35

These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

Mapping and Sequencing Two deb-1 Mutations

R.J. Barstead and R.H. Waterston

The deb-1 gene has been cloned, sequenced, mapped to chromosome IV 
close to unc-44, and shown to encode the protein vinculin (1).  The 
postulated function of vinculin in vertebrate muscle and non-muscle 
cells is to control the position and stability of the attachment of 
actin filaments to the membrane (2).  In nematodes vinculin is found 
at the base of the muscle dense-bodies linking the thin filaments to 
the membrane, an analogous position to that in vertebrate tissues.  In 
order to asses its function in the nematode we sought to recover 
mutations in the deb-1 gene.  Since there were no known muscle Uncs in 
the region of deb-1, we suspected that mutations in the gene would be 
lethal, with morphology and behavior like that of lethal myo-3 mutants 
(3).  We have now recovered two mutants with such a phenotype which 
map close to unc-44.  One, deb-1(st555), does not express any vinculin 
as assayed by immunofluorescence of arrested embryos.  The second, deb-
1(st385), expresses vinculin at a reduced level compared to wild type 
worms.
Two recent methodologies made it feasible to recover DNA from 
arrested deb-1 mutants, locate the position of the mutations in the 
gene, and sequence the mutated site.  To recover DNA from the mutant 
gene, arrested animals were picked off plates, digested with 
Proteinase K, and PCR fragments were made which covered all of the 
coding sequence.  To map the position of the mutated site, the PCR 
fragments were mixed with corresponding end-labeled fragments from 
wild type DNA, denatured, and allowed to hybridize to generate 
heteroduplexes.  The heteroduplexes were treated with hydroxylamine 
which results in the modification of any mismatched cytosine.  
Cleavage of the modified cytosines with piperidine followed by 
fractionation of the products on denaturing acrylamide gels allowed us 
to position and subsequently to sequence the mutations.  The mutation 
deb-1(st555) was found to represent a change in a conserved G in a 
splice acceptor site adjacent to exon five, and deb-1(st385) was found 
to represent the introduction of an amber stop codon in exon eight.  
We have subsequently shown that sup-7 will rescue the early arrest 
phenotype of st385, yielding adults with disorganized muscle.  We are 
currently attempting to rescue the mutant by transformation with a 
wild type copy of the deb-1 gene.