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  Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of class I myosin

Fujita-Becker, S., Dürrwang, U., Erent, M., Clark, R., Geeves, M. A., & Manstein, D. J. (2005). Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of class I myosin. The Journal of Biological Chemistry, 280(7), 6064-6071. doi:10.1074/jbc.M412473200.

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Genre: Journal Article
Alternative Title : Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of class I myosin

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JBiolChem_280_2005_6064.pdf (Any fulltext), 319KB
 
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 Creators:
Fujita-Becker, Setsuko1, Author              
Dürrwang, Ulrike1, Author              
Erent, Muriel1, Author              
Clark, Richard, Author
Geeves, Michael A., Author
Manstein, Dietmar J.1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: Class I myosins are single-headed motor proteins implicated in various motile processes including organelle translocation, ion channel gating, and cytoskeleton reorganization. Dictyostelium discoideum myosin-ID belongs to subclass 1alpha, whose members are thought to be tuned for rapid sliding. The direct analysis of myosin-ID motor activity is made possible by the production of single polypeptide constructs carrying an artificial lever arm. Using these constructs, we show that the motor activity of myosin-ID is activated 80-fold by phosphorylation at the TEDS site. TEDS site phosphorylation acts by stabilizing the actomyosin complex and increasing the coupling between actin binding and the release of hydrolysis products. A surprising effect of Mg(2+) ions on in vitro motility was discovered. Changes in the level of free Mg(2+) ions within the physiological range are shown to modulate motor activity by inhibiting ADP release. Our results indicate that higher concentrations of free Mg(2+) ions stabilize the tension-bearing actin myosin ADP state and shift the system from the production of rapid movement toward the generation of tension.

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Language(s): eng - English
 Dates: 2004-11-262004-11-042004-12-042004-12-042005-02-18
 Publication Status: Published in print
 Pages: 8
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 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 280 (7) Sequence Number: - Start / End Page: 6064 - 6071 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1