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  Differences in the ionic interaction of actin with the motor domains of nonmuscle and muscle myosin II

Van Dijk, J., Furch, M., Derancourt, J., Batra, R., Knetsch, M. L. W., Manstein, D. J., et al. (1999). Differences in the ionic interaction of actin with the motor domains of nonmuscle and muscle myosin II. European Journal of Biochemistry, 260(3), 672-683.

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EurJBiochem_260_1999_672.pdf (Any fulltext), 537KB
 
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 Creators:
Van Dijk, Juliette, Author
Furch, Marcus1, Author              
Derancourt, Jean, Author
Batra, Renu1, Author              
Knetsch, Menno L. W.1, Author              
Manstein, Dietmar J.1, Author              
Chaussepied, Patrick, Author
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: actin; myosin; actomyosin interface; cross-linking; proteolysis; adenosinetriphosphatase; mutagenesis
 Abstract: Changes in the actin-myosin interface are thought to play an important role in microfilament-linked cellular movements. In this study, we compared the actin binding properties of the motor domain of Dictyostelium discoideum (M765) and rabbit skeletal muscle myosin subfragment-1 (S1). The Dictyostelium motor domain resembles S1(A2) (S1 carrying the A2 light chain) in its interaction with G-actin. Similar to S1(A2), none of the Dictyostelium motor domain constructs induced G-actin polymerization. The affinity of monomeric actin (G-actin) was 20-fold lower for M765 than for S1(A2) but increasing the number of positive charges in the loop 2 region of the D. discoideum motor domain (residues 613-623) resulted in equivalent affinities of G-actin for M765 and for S1. Proteolytic cleavage and cross-linking approaches were used to show that M765, like S1, interacts via the loop 2 region with filamentous actin (F-actin). For both types of myosin, F-actin prevents trypsin cleavage in the loop 2 region and F-actin segment 1-28 can be cross-linked to loop 2 residues by a carbodiimide-induced reaction. In contrast with the S1, loop residues 559-565 of D. discoideum myosin was not cross-linked to F-actin, probably due to the lower number of positive charges. These results confirm the importance of the loop 2 region of myosin for the interaction with both G-actin and F-actin, regardless of the source of myosin. The differences observed in the way in which M765 and S1 interact with actin may be linked to more general differences in the structure of the actomyosin interface of muscle and nonmuscle myosins

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Language(s): eng - English
 Dates: 1998-12-081998-09-171998-12-082001-12-251999-03-01
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: Other: 8041
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 260 (3) Sequence Number: - Start / End Page: 672 - 683 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040