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dc.contributor.advisorDu, Shaojunen_US
dc.contributor.authorXu, Jinen_US
dc.date.accessioned2012-10-11T05:43:30Z
dc.date.available2012-10-11T05:43:30Z
dc.date.issued2012en_US
dc.identifier.urihttp://hdl.handle.net/1903/13150
dc.description.abstractMyofibrillogenesis, the process of sarcomere formation, requires close interaction of sarcomeric proteins and molecular chaperones. Smyd1 is a lysine methyltransferase that plays important roles in myofibrillogenesis in both skeletal and cardiac muscles. Knockdown of smyd1 results in complete disruption of sarcomere organization. The molecular mechanism by which Smyd1 controls myofibril assembly is not clear. In this study, we analyzed the sub-cellular localization of Smyd1, the effect of smyd1 knockdown on protein methylation, and the effect of myomesin knockdown on sarcomere organization. We demonstrated that Smyd1b_tv1 is localized to the M-lines of skeletal muscles in zebrafish embryos. Knockdown of myomesin-1b or myomesin-3 had no effect on the sarcomere organization. Western blot analysis revealed that knockdown of smyd1 reduced the overall protein methylation in zebrafish embryos. Together, these studies indicate that Smyd1 is required for M-line organization and Smyd1 may play a role in protein methylation and is involved in sarcomere assembly.en_US
dc.titleFunctional analysis of Smyd1 and Myomesin in sarcomere organization in zebrafish embryosen_US
dc.typeThesisen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.contributor.departmentMarine-Estuarine-Environmental Sciencesen_US
dc.subject.pqcontrolledBiologyen_US
dc.subject.pqcontrolledGeneticsen_US
dc.subject.pqcontrolledDevelopmental biologyen_US
dc.subject.pquncontrolledMuscleen_US
dc.subject.pquncontrolledMyomesinen_US
dc.subject.pquncontrolledSarcomereen_US
dc.subject.pquncontrolledSmyd1en_US
dc.subject.pquncontrolledZebrafishen_US


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