Literature DB >> 6615456

The polymerization of actin. A study of the nucleation reaction.

E Grazi, A Ferri, S Cino.   

Abstract

We compared the properties of the nuclei that accumulate in 7.5 mM-KCl in ATP-G-actin solutions and of the oligomers that are formed by sonication of either G-actin or F-actin. We found that the ability of the above species to prime the polymerization of actin decays with different rates. The nuclei are stable in 7.5 mM-KCl (they decay with a rate constant of 1.5 X 10(-3) s -1 at pH 7.8 at 22 degrees C in the absence of KCl). The oligomers formed by sonication of either G-actin or F-actin, once the sonication is stopped, revert to simpler structures or evolve into F-actin, depending on the KCl concentration in which they are kept. In 10.5 mM-KCl at pH 7.8 at 22 degrees C their priming ability decays with a rate constant of 6 X 10(-3) s -1. We propose that the nuclei that form spontaneously in 7.5 mM-KCl are not directly susceptible to elongation. They must first be converted into activated nuclei, which exist in very low concentration at the steady state. The activated nuclei are directly susceptible to elongation, they have a short life and they decay rapidly into the ground state unless the elongation reaction occurs. Sonication displaces the steady-state concentration in favour of the activated state.

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Year:  1983        PMID: 6615456      PMCID: PMC1152189          DOI: 10.1042/bj2130727

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


  8 in total

1.  The cooperative nature of G-F transformation of actin.

Authors:  M KASAI; S ASAKURA; F OOSAWA
Journal:  Biochim Biophys Acta       Date:  1962-02-12

2.  Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin.

Authors:  D J Gordon; Y Z Yang; E D Korn
Journal:  J Biol Chem       Date:  1976-12-10       Impact factor: 5.157

3.  Detection of conformational changes in actin by proteolytic digestion: evidence for a new monomeric species.

Authors:  S A Rich; J E Estes
Journal:  J Mol Biol       Date:  1976-07-15       Impact factor: 5.469

4.  Control of rabbit liver fructose-1, 6-diphosphatase activity by magnesium ions.

Authors:  Y Tashima; N Yoshimura
Journal:  J Biochem       Date:  1975-12       Impact factor: 3.387

5.  The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.

Authors:  J A Spudich; S Watt
Journal:  J Biol Chem       Date:  1971-08-10       Impact factor: 5.157

6.  The first step in the polymerisation of actin.

Authors:  J F Rouayrenc; F Travers
Journal:  Eur J Biochem       Date:  1981-05

7.  Mechano-chemical energy transduction in biological systems. The effect of mechanical stimulation on the polymerization of actin: a kinetic study.

Authors:  A Ferri; E Grazi
Journal:  Biochem J       Date:  1982-08-01       Impact factor: 3.857

8.  The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence.

Authors:  J H Collins; M Elzinga
Journal:  J Biol Chem       Date:  1975-08-10       Impact factor: 5.157

  8 in total
  5 in total

1.  Self-assembly properties of a model RING domain.

Authors:  Alex Kentsis; Ronald E Gordon; Katherine L B Borden
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-15       Impact factor: 11.205

2.  An alternative pathway of actin filament elongation. The condensation of small oligomers.

Authors:  E Grazi
Journal:  J Muscle Res Cell Motil       Date:  1989-08       Impact factor: 2.698

3.  Kinetic heterogeneity of F-actin polymers. Further evidence that the elongation reaction may occur through condensation of the actin filaments with small aggregates.

Authors:  E Grazi; E Magri
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

4.  Characterization of the ATP-G-actin aggregates formed at low potassium chloride concentration.

Authors:  E Grazi; A Aleotti; A Ferri
Journal:  Biochem J       Date:  1984-04-01       Impact factor: 3.857

5.  54Mn2+ as a tracer of the polymerization of actin. Intermediate oligomers condense to give F-actin.

Authors:  E Grazi
Journal:  Biochem J       Date:  1984-11-01       Impact factor: 3.857

  5 in total

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