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| Subject Categories: Membranes & Transport | Plant Biology |
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| The EMBO Journal
(2003) 22, 450–458, doi:10.1093/emboj/cdg036 |
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| A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core |
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| Friederike Schäfer1, Dominga Deluca2, Ulrike Majdic1, Joachim Kirchner1, Manfred Schliwa1, Luis Moroder2 and Günther Woehlke1 |
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1 Adolf Butenandt Institute, Cell Biology, University of Munich, Schillerstra e 42, D-80336 Munich, Germany2 Max Planck Institute for Biochemistry, Department of Bioorganic Chemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany To whom correspondence should be addressed Günther Woehlke, guenther.woehlke@lrz.uni-muenchen.de Received 24 May 2002; Revised 14 October 2002; Accepted 22 November 2002. |
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| Abstract |
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| 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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| Keywords: ATPase kinetics, conventional kinesin, dimerization, neck domain, synthetic peptides |
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