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Cloning and expression of kinesins from the thermophilic fungus Thermomyces lanuginosus

Published online by Cambridge University Press:  01 December 1999

ROMAN SAKOWICZ ,
SAM FARLOW  and
LAWRENCE S.B. GOLDSTEIN
ROMAN SAKOWICZ
Affiliation:
Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0683 Present address: Cytokinetics, Inc., 280 East Grand Avenue, Suite 2, South San Francisco, California 94080.
SAM FARLOW
Affiliation:
Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0683
LAWRENCE S.B. GOLDSTEIN
Affiliation:
Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0683
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Abstract

The motor domain regions of three novel members of the kinesin superfamily TLKIF1, TLKIFC, and TLBIMC were identified in a thermophilic fungus Thermomyces lanuginosus. Based on sequence similarity, they were classified as members of the known kinesin families Unc104/KIF1, KAR3, and BIMC. TLKIF1 was subsequently expressed in Escherichia coli. The expression level was high, and the protein was mostly soluble, easy to purify, and enzymatically active. TLKIF1 is a monomeric kinesin motor, which in a gliding motility assay displays a robust plus-directed microtubule movement up to 2 μm/s. The discovery of TLKIF1 also demonstrates that a family of kinesin motors not previously found in fungi may in fact be used in this group of organisms.

Keywords

intracellular motilitykinesinmicrotubulesmotor proteinthermomyces
Type
Research Article
Information
Protein Science , Volume 8 , Issue 12 , December 1999 , pp. 2705 - 2710
Copyright
© 1999 The Protein Society

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