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Access through your institution Buy or subscribe Kinesin and non-claret disjunctional (ncd) are molecular motors of the kinesin superfamily that move in opposite directions along

microtubules. The molecular basis underlying the direction of movement is unclear, although it is thought to be an intrinsic property of the motor domain, a conserved region about 330 amino

acids in length1,2,3. The motor domain is found at the amino terminus in conventional kinesins, but at the carboxy terminus in ncd4,5. Here we report on a chimaera composed of the motor

domain of the minus-end-directed kinesin of _Neurospora crassa_6. The bacterially expressed fusion protein was tested in motility assays using polarity-marked microtubules7. Surprisingly,

the chimaera moved towards the plus end, demonstrating that the polarity of force generation of the ncd motor domain has been reversed. This finding indicates that the domain organization,

particularly the position of the motor domain, is of fundamental importance for the polarity of force production. It also demonstrates that the direction of microtubule movement is not

controlled solely by the motor domain8. The identity of this polypeptide was investigated in immunoblots using a polyclonal antibody against the Nkin stalk/tail domain6 and a peptide

antibody (MMR48) against a consensus sequence 24 amino acids in length in the HIPYR region of animal kinesins13. The Nkin antibody recognized Nkin as well as the chimaera, but not GST–MC5

(ncd). Antibody MMR48 reacted strongly with Nkin, which was to be expected given the high degree of sequence conservation of the HIPYR peptide between animal kinesins and Nkin. Its reaction

with GST–MC5, however, was much weaker, because of considerable sequence divergence in the HIPYR peptide between ncd and animal kinesins. The chimaera showed the same weak reaction with

MMR48 as GST–MC5. Thus the chimaera combines the immunological characteristics of the Nkin stalk/tail domain and the ncd motor domain. This is a preview of subscription content, access via

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* Learn about institutional subscriptions * Read our FAQs * Contact customer support REFERENCES * Bloom, G. & Endow, S. Motor proteins 1: kinesin. _Prot. Profiles_ 1, 1059–1116 (1994).

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451–453 (1996). Article  ADS  CAS  Google Scholar  Download references ACKNOWLEDGEMENTS We thank S. Endow for the GST–MC5 clone; M. McNiven for the MMR48 antibody; M. Fritz for the

rhodamine-labelled tubulin; U. Euteneuer, H. Felgner, R. Gräf and S. Linder for advice; and S. Fuchs for technical assistance. This work was supported by a Graduiertenkolleg fellowship to

U.H. and a grant from the DFG to M.S. AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Adolf-Butenandt-Institut, Zellbiologie, University of Munich, Schillerstrasse 42, Munich, 80336, Germany

Ulrike Henningsen & Manfred Schliwa Authors * Ulrike Henningsen View author publications You can also search for this author inPubMed Google Scholar * Manfred Schliwa View author

publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence to Manfred Schliwa. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS

ARTICLE CITE THIS ARTICLE Henningsen, U., Schliwa, M. Reversal in the direction of movement of a molecular motor. _Nature_ 389, 93–96 (1997). https://doi.org/10.1038/38022 Download citation

* Received: 11 June 1997 * Accepted: 16 July 1997 * Issue Date: 04 September 1997 * DOI: https://doi.org/10.1038/38022 SHARE THIS ARTICLE Anyone you share the following link with will be

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