Worm Breeder's Gazette 11(2): 34
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.
More molecular analysis has been done with kind supply of unc-15 mutants (CGC, Don Riddle, Ann Rose). Four mutation sites(e1402; temperature sensitive, e1215; weak allele, m208 and m209; e73 intragenic revertants) were located on, or near the weak spot of C- terminal end of the paramyosin. We have already shown that one point mutation with charge reversion dramatically change thick filament assembly and behavior of the animal (The last C. elegans meeting and the gazette vol.12#1). Amino acid substitutions were localized on the C-terminal end. This suggests that this region might be important in the initiation of the filament assembly and the total charge interaction between molecules might function on the final stability of the thick filament. Paramyosin has two weak spots on N- and C- terminal, and N-terminal spot also exists in the myosin heavy chain B. Therefore, C-terminal weak spot might be related to paramyosin specific functions. Our recent results should be understood together with biological functions of helical domain of other proteins; DNA binding proteins, transmembrane domain of receptor and/or channel protein growth factors. Helices may play biologically important rules not only in DNA but also in proteins. [See Figure 1]