Literature DB >> 1710551

Heterodimeric capping proteins constitute a highly conserved group of actin-binding proteins.

H Hartmann1, M Schleicher, A A Noegel.   

Abstract

The two subunits of the heterodimeric protein cap32/34, an actin-binding protein, are encoded by separate single-copy genes. We have established the genomic structure of both genes. A sequence comparison of cap32/34 with capZ from chicken skeletal muscle and two partially known sequences from Saccharomyces cerevisiae and Xenopus laevis show that heterodimeric capping proteins belong to a highly conserved group of actin-binding proteins. This conclusion is supported by the cross-reaction of polyclonal antibodies against cap32 and cap34 with proteins from lower and higher eukaryotes. In addition, a system is presented that allows the expression of truncated cap34 polypeptides under the control of the cap34 promoter.

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Year:  1990        PMID: 1710551     DOI: 10.1002/dvg.1020110508

Source DB:  PubMed          Journal:  Dev Genet        ISSN: 0192-253X


  4 in total

1.  Actin filament barbed-end capping activity in neutrophil lysates: the role of capping protein-beta 2.

Authors:  M J DiNubile; L Cassimeris; M Joyce; S H Zigmond
Journal:  Mol Biol Cell       Date:  1995-12       Impact factor: 4.138

Review 2.  The Dictyostelium cytoskeleton.

Authors:  A A Noegel; J E Luna
Journal:  Experientia       Date:  1995-12-18

3.  Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum.

Authors:  Christian Eckert; Agnieszka Goretzki; Maria Faberova; Martin Kollmar
Journal:  BMC Struct Biol       Date:  2012-06-01

4.  The heat shock cognate protein from Dictyostelium affects actin polymerization through interaction with the actin-binding protein cap32/34.

Authors:  U Haus; P Trommler; P R Fisher; H Hartmann; F Lottspeich; A A Noegel; M Schleicher
Journal:  EMBO J       Date:  1993-10       Impact factor: 11.598

  4 in total

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