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dc.contributor.advisorWollenberg, Amanda C.
dc.contributor.authorWaalkes, Erika K.
dc.date.accessioned2018-09-22T18:19:53Z
dc.date.available2018-09-22T18:19:53Z
dc.date.issued2018
dc.identifier.urihttp://hdl.handle.net/10920/35987
dc.descriptionvi, 58 p.en_US
dc.description.abstractMyosin is a protein found within thick filaments of muscle myofibrils, functioning in the contraction and relaxation of muscles. In Caenorhabditis eiegans myosin is found within a highly organized contractile apparatus in the body wall muscles. The apparatus is composed of thin filaments containing actin and thick filaments containing both myosin A (myo-3) and myosinB {unc-54). The myosin A protein of C. eiegans body wall muscle contains multiple regions of amino acid residues that are highly conserved in the myosin of other organisms. Using C. eiegans strains generated through the Million Mutation Project, this study is first to characterize the phenotype of point mutations in the myo-3 gene, which encodes for the highly conserved myosin heavy chain A (MHC A) motor domain region. The characterization showed that double mutants homozygous for the myo-3 G234D [myo-3(gk656293)] point mutation and null for myosin B [unc-54(el90)] are not viable with larvae arresting in the early hours of embryonic development. Whereas both single homozygous mutants are viable with no obvious embryonic lethality. Taken together these results indicate that, unlike wild-type myo-3-, mutant myo-3 G234D cannot compensate for the loss of myosin B and likely has a dominant role in early embryonic assembly. Single mutants of myo-3 G234D were viable, but antibody embryo stains revealed delayed organization and localization of MHC A in filaments. The results presented in this study implicate MHC A motor domain's role in early embryonic muscle development and organization of thick filaments. The role of MHC A has the potential to have much broader implications like contractile heart diseases such as cardiomyopathy, becauseMYO2 within human cardiac myofibrils have these same conserved amino acids.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Biology Senior Individualized Projects Collection
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.
dc.titleMyosin Motor Domains Perform Distinct Functions in Caenorhabditis eiegans Body Wall Muscleen_US
dc.typeThesisen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email dspace@kzoo.edu to request access to this thesis.


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  • Biology Senior Individualized Projects [1520]
    This collection includes Senior Individualized Projects (SIP's) completed in the Biology Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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