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Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure

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Title: Characterization of short ADP ribosylated oligomers developed by modification in F-actin structure
Author: Mishra, Vadika
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: Dawson, John
Abstract: Researchers have been trying to determine the mechanism of the crossbridge cycle, containing actomyosin complex, formed by the interaction of F-actin and myosin. But, because actin forms polymers of varying lengths, it has been difficult to crystallize this complex. My research is aimed at developing a homogeneous actomyosin complex with a short actin oligomer that possesses one myosin-binding site. ADPr-oligomers are produced by chemical crosslinking of F-actin and inhibiting polymerization by ADP-ribosylation. Specifically, I determined the behavior of an ADPr-trimer and dimer with myosin and its effect on actomyosin activity. Individual myosin ATPase activities of ADPr-trimer/dimer were similar to basal myosin activity. However, in the presence of long ADPr-oligomers (tetramer, pentamer, etc.) or F-actin, ADPr-dimer/trimer show binding and activity with myosin thick filaments. Thus, I was unable to produce a short actomyosin complex through these efforts and present a model for interaction of short actin oligomers with each other in the presence of long actin filaments and myosin.
Description: We tried to modify F-actin to build a complex with myosin and generate an actomyosin complex suitable for crystal studies
URI: http://hdl.handle.net/10214/8714
Date: 2015-01
Rights: Attribution-NonCommercial-NoDerivs 2.5 Canada
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Attribution-NonCommercial-NoDerivs 2.5 Canada Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 2.5 Canada