Evidence for myosin in Tetrahymena.
Item
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Title
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Evidence for myosin in Tetrahymena.
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Identifier
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AAI9707092
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identifier
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9707092
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Creator
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Garces, Jorge Alberto.
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Contributor
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Adviser: R. H. Gavin
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Date
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1996
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biology, Cell | Biology, Molecular
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Abstract
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The objective of this study was to provide evidence for myosin in Tetrahymena. A combination of immunochemical, biochemical and PCR-based approaches have been employed to identify myosin-like proteins and myosin gene sequences.;Anti-myosin antibodies were affinity-purified from an antiserum raised against a Tetrahymena cytoskeletal protein fraction. The anti-myosin antibodies detected a 180 kD protein on western blots and immunoprecipitated the polypeptide from cytoskeletal protein fractions. The 180 kD protein exhibited an ATPase activity characteristic of myosins and was shown to bind skeletal muscle actin filaments in an ATP-dependent fashion. Immunofluorescence and immunogold electron microscopy were used to localize the p-180 to basal-body associated fibrillar structures and other cell constituents.;PCR-based screens for myosin in Tetrahymena have identified a sequence that shares a high degree of homology to other myosins. Alignment of the deduced amino acid sequence from approximately 2,000 bp of the Tetrahymena sequence with myosin consensus sequences revealed several shared conserved amino acid regions. Based on these amino acid alignments, we have concluded that the PCR-based screen has detected TETMYO-1, the first myosin gene in Tetrahymena.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
