Worm Breeder's Gazette 1(2): 24
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.
Native myosins from N2, E675, E190, E569, R73, E651, and R74 have been purified (1) from two growths of each strain, and each purified preparation was independently cleaved by cyanogen bromide. (We are now on our third run through.) The peptides have been separated on 8M ureasodium dodecyl sulfate polyacrylamide gels and/or a two- dimensional system with gel electro-focusing in 8M urea as the first dimension (2). N2 and E675 myosins are virtually indistinguishable by these methods. The peptide compositions of E190, E569, and E651 all resemble the map of the normal molecular weight heavy chain of E675, suggesting the partial or complete absence of the unc 54-affected chain. R73 and R74 are partially paralyzed, muscle defective, EMS- induced phenotypic revertants of E569 and E651 (3). The myosins of these strains are very similar to N2. However, two-dimensional separation of R73 myosin peptides suggests that two fragments are uniquely present. Further work is proceeding on this and other mutant myosins. The observation with R73 strongly suggests that the E569 mutation within unc 54 affects a coding region.