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  A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core

Schäfer, F., Deluca, D., Majdic, U., Kirchner, J., Schliwa, M., Moroder, L., et al. (2003). A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core. EMBO Journal, 22(3), 450-458.

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Genre: Journal Article
Alternative Title : Embo J.

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 Creators:
Schäfer, F., Author
Deluca, D.1, Author              
Majdic, U., Author
Kirchner, J., Author
Schliwa, M., Author
Moroder, L.1, Author              
Woehlke, G., Author
Affiliations:
1Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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Free keywords: ATPase kinetics; conventional kinesin; dimerization; neck domain; synthetic peptides
 Abstract: The neck domain of fungal conventional kinesins displays characteristic properties which are reflected in a specific sequence pattern. The exchange of the strictly conserved Tyr 362, not present in animals, into Lys, Cys or Phe leads to a failure to dimerize. The destabilizing effect is confirmed by a lower coiled-coil propensity of mutant peptides. Whereas the Phe substitution has only a structural effect, the Lys and Cys replacements lead to dramatic kinetic changes. The steady state ATPase is 4- to 7-fold accelerated, which may be due to a faster microtubule-stimulated ADP release rate. These data suggest that an inhibitory effect of the fungal neck domain on the motor core is mediated by direct interaction of the aromatic ring of Tyr 362 with the head, whereas the OH group is essential for dimerization. This is the first demonstration of a direct influence of the kinesin neck region in regulation of the catalytic activity.

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Language(s): eng - English
 Dates: 2003-02-03
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 35292
ISI: 000181030200010
 Degree: -

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Title: EMBO Journal
  Alternative Title : Embo J.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 22 (3) Sequence Number: - Start / End Page: 450 - 458 Identifier: ISSN: 0261-4189