Event Title
Characterizing Temperature-Sensitive Mutations in Caenorhabditis elegans Myosin (Unc-54)
Location
Science Center, Bent Corridor
Start Date
10-2-2015 12:00 PM
End Date
10-2-2015 1:20 PM
Poster Number
42
Abstract
Myosin 4, encoded by the gene unc-54, functions in the body wall muscle of the nematode C. elegans. In both nematode and human muscles, myosin is the motor in the force-generating powerstroke, which converts a chemical signal to mechanical energy. My research this summer aimed to characterize the genetic and physiological consequences of two temperature-sensitive mutations in the myosin head. More specifically, I explored whether the mutations’ phenotypic effects resulted from the reduced production of functional myosin or from the production of a poison myosin peptide, and whether the changes induced by an increase in temperature occurred developmentally or functionally. Using mechanical models for C. elegans movement, and polarized light microscopy of myosin filaments, I examined the phenotypic effects of the mutations e1301 and e1157 under different temperature conditions, and found evidence for dominant or semidominant behavior.
Recommended Citation
Campbell, Amy, "Characterizing Temperature-Sensitive Mutations in Caenorhabditis elegans Myosin (Unc-54)" (2015). Celebration of Undergraduate Research. 42.
https://digitalcommons.oberlin.edu/cour/2015/posters/42
Major
Biology
Project Mentor(s)
Taylor Allen, Biology
Document Type
Poster
Characterizing Temperature-Sensitive Mutations in Caenorhabditis elegans Myosin (Unc-54)
Science Center, Bent Corridor
Myosin 4, encoded by the gene unc-54, functions in the body wall muscle of the nematode C. elegans. In both nematode and human muscles, myosin is the motor in the force-generating powerstroke, which converts a chemical signal to mechanical energy. My research this summer aimed to characterize the genetic and physiological consequences of two temperature-sensitive mutations in the myosin head. More specifically, I explored whether the mutations’ phenotypic effects resulted from the reduced production of functional myosin or from the production of a poison myosin peptide, and whether the changes induced by an increase in temperature occurred developmentally or functionally. Using mechanical models for C. elegans movement, and polarized light microscopy of myosin filaments, I examined the phenotypic effects of the mutations e1301 and e1157 under different temperature conditions, and found evidence for dominant or semidominant behavior.