Literature DB >> 1849405

Definition of a Ca2(+)-sensitive interface in the plasma gelsolin-actin complex.

A Houmeida1, V Hanin, J Feinberg, Y Benyamin, C Roustan.   

Abstract

Gelsolin is a Ca2(+)-dependent protein which severs actin filaments, caps their fast-growing ends and promotes nucleation. We report here results that delimit one of the interfaces between serum gelsolin and actin monomer. An actin-derived synthetic peptide (amino acids 305-326 of actin) coupled to a hydrophilic resin was tested for its possible interaction with gelsolin. We selected this sequence because it corresponds to a region implicated in the gelsolin-actin complex in a previous work [Boyer, Feinberg, Hue, Capony, Benyamin & Roustan (1987) Biochem. J. 248, 359-364]. We showed that this actin sequence is located at the surface of the actin molecule and observed a Ca2(+)-sensitive binding of gelsolin to this actin-derived peptide. In addition, by using a chymotryptic digest of gelsolin, we reported that only the C-terminal half of gelsolin interacts with the actin-(305-326)-peptide. These results that the Ca2(+)-sensitive interface includes both amino acids 305-326 of actin and probably amino acids 660-738 of gelsolin.

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Year:  1991        PMID: 1849405      PMCID: PMC1149975          DOI: 10.1042/bj2740753

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  29 in total

1.  Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains.

Authors:  E André; F Lottspeich; M Schleicher; A Noegel
Journal:  J Biol Chem       Date:  1988-01-15       Impact factor: 5.157

Review 2.  Gelsolin: calcium- and polyphosphoinositide-regulated actin-modulating protein.

Authors:  H L Yin
Journal:  Bioessays       Date:  1987-10       Impact factor: 4.345

3.  Preparation and characterization of bovine aortic actin.

Authors:  J C Cavadore; C Axelrud-Cavadore; P Berta; M C Harricane; J Haiech
Journal:  Biochem J       Date:  1985-06-01       Impact factor: 3.857

4.  Plasma-gelsolin-binding sites on the actin sequence.

Authors:  Y Doi; M Higashida; S Kido
Journal:  Eur J Biochem       Date:  1987-04-01

5.  End-label fingerprintings show that the N- and C-termini of actin are in the contact site with gelsolin.

Authors:  K Sutoh; H L Yin
Journal:  Biochemistry       Date:  1989-06-13       Impact factor: 3.162

6.  Muscle is the major source of plasma gelsolin.

Authors:  D J Kwiatkowski; R Mehl; S Izumo; B Nadal-Ginard; H L Yin
Journal:  J Biol Chem       Date:  1988-06-15       Impact factor: 5.157

7.  The binary complex of pig plasma gelsolin with Mg2+-G-actin in ATP and ADP.

Authors:  H E Harris
Journal:  FEBS Lett       Date:  1988-06-20       Impact factor: 4.124

8.  Identification of critical functional and regulatory domains in gelsolin.

Authors:  D J Kwiatkowski; P A Janmey; H L Yin
Journal:  J Cell Biol       Date:  1989-05       Impact factor: 10.539

9.  The actin filament-severing domain of plasma gelsolin.

Authors:  C Chaponnier; P A Janmey; H L Yin
Journal:  J Cell Biol       Date:  1986-10       Impact factor: 10.539

10.  Gelsolin has three actin-binding sites.

Authors:  J Bryan
Journal:  J Cell Biol       Date:  1988-05       Impact factor: 10.539

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  1 in total

1.  Definition of the EGTA-independent interface involved in the serum gelsolin-actin complex.

Authors:  J Feinberg; J P Capony; Y Benyamin; C Roustan
Journal:  Biochem J       Date:  1993-08-01       Impact factor: 3.857

  1 in total

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