Literature DB >> 544931

Structural states of dictyostelium myosin.

P R Stewart, J A Spudich.   

Abstract

Myosin purified from Dictyostelium amoebae has approximately 10% by weight of RNA associated with it, unless specific steps (DEAE cellulose chromatography or RNase digestion) are taken to remove it. This RNA has significant effects on the structural states formed by the myosin at low ionic strength in the presence of Mg2+. Rapid precipitation of RNA-free myosin by dilution generates bipolar thick filaments (540 nm long, 33 nm thick), often with a bare zone and a 15-nm transverse repeat. Rapid precipitation of myosin with copurified RNA yields linear aggregates of bipolar filaments, showing some lateral association. Slow precipitation of RNA-free myosin by dialysis yields very long filaments or ribbons (greater than 5 micrometer, 30--60 nm wide) in which the myosin may be packed diagonally across the filament, similar to the "side-polar" aggregates formed by other nonmuscle myosins and by smooth muscle myosin (Craig R, Megerman J: J Cell Biol 75:990, 1977; Hinssen H, D'Haese J, Small JV, Sobieszek A: J Ultrastruct Res 64:282, 1978). Slow precipitation of myosin with copurified RNA generates linear filaments with repeat intervals of 290 and 650 nm. Other polyanions were tested for their effects on myosin aggregation. Total RNA and ribosomal RNA from Dictyostelium, when added to RNA-free myosin, also induced the extensive linear aggregation seen with the copurified RNA/myosin complex, although higher concentrations of RNA were required to obtain quantitatively the same effect. DNA and heparin were also effective inducers of linear aggregation, whereas homopolymers of nucleotides and of acidic or basic amino acids were poorly effective.

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Year:  1979        PMID: 544931     DOI: 10.1002/jss.400120102

Source DB:  PubMed          Journal:  J Supramol Struct        ISSN: 0091-7419


  9 in total

1.  Temperature dependence of myosin-II tail fragment assembly.

Authors:  Peggy M McMahon; Daniel R Hostetter; Sarah E Rice
Journal:  J Muscle Res Cell Motil       Date:  2008-09-11       Impact factor: 2.698

2.  Actin filaments mediate Dictyostelium myosin assembly in vitro.

Authors:  R K Mahajan; K T Vaughan; J A Johns; J D Pardee
Journal:  Proc Natl Acad Sci U S A       Date:  1989-08       Impact factor: 11.205

3.  Expression in Escherichia coli of a functional Dictyostelium myosin tail fragment.

Authors:  A De Lozanne; C H Berlot; L A Leinwand; J A Spudich
Journal:  J Cell Biol       Date:  1987-12       Impact factor: 10.539

4.  Monoclonal antibodies binding to the tail of Dictyostelium discoideum myosin: their effects on antiparallel and parallel assembly and actin-activated ATPase activity.

Authors:  K Pagh; G Gerisch
Journal:  J Cell Biol       Date:  1986-10       Impact factor: 10.539

5.  Myosin filament structure in vertebrate smooth muscle.

Authors:  J Q Xu; B A Harder; P Uman; R Craig
Journal:  J Cell Biol       Date:  1996-07       Impact factor: 10.539

6.  Expression of Dictyostelium myosin tail segments in Escherichia coli: domains required for assembly and phosphorylation.

Authors:  T J O'Halloran; S Ravid; J A Spudich
Journal:  J Cell Biol       Date:  1990-01       Impact factor: 10.539

7.  Intermolecular versus intramolecular interactions of Dictyostelium myosin: possible regulation by heavy chain phosphorylation.

Authors:  C Pasternak; P F Flicker; S Ravid; J A Spudich
Journal:  J Cell Biol       Date:  1989-07       Impact factor: 10.539

8.  The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps.

Authors:  J H Sinard; W F Stafford; T D Pollard
Journal:  J Cell Biol       Date:  1989-10       Impact factor: 10.539

9.  Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod.

Authors:  Daniel Hostetter; Sarah Rice; Sara Dean; David Altman; Peggy M McMahon; Shirley Sutton; Ashutosh Tripathy; James A Spudich
Journal:  PLoS Biol       Date:  2004-10-19       Impact factor: 8.029

  9 in total

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