Source:http://linkedlifedata.com/resource/pubmed/id/18160177
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2008-3-24
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pubmed:abstractText |
The amoeba Dictyostelium discoideum possesses genes for 13 different kinesins. Here we characterize DdKif3, a member of the Kinesin-1 family. Kinesin-1 motors form homodimers that can move micrometer-long distances on microtubules using the energy derived from ATP hydrolysis. We expressed recombinant motors in Escherichia coli and tested them in different in vitro assays. Full-length and truncated Kif3 motors were active in gliding and ATPase assays. They showed a strong dependence on ionic strength. Like the full-length motor, the truncated DdKif3-592 motor (aa 1-592; comprising motor domain, neck, and partial stalk) reached its maximum speed of around 2.0micrcom s(-1) at a potassium acetate concentration of 200mM. The shortened DdKif3-342 motor (aa 1-342; comprising motor domain, partial neck) showed a high ATP turnover, comparable to that of the fungal Kinesin-1, Nkin. Results from the duty cycle calculations and gliding assays indicate that DdKif3 is a processive motor. A GFP-fusion protein revealed a mainly cytoplasmic localization of DdKif3. Immunofluorescence staining makes an association with the endoplasmic reticulum or mitochondria unlikely. Despite a similar phylogenetic distance to both metazoa and fungi, in terms of its biochemical properties DdKif3 revealed a closer similarity to fungal than animal kinesins.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Kinesin,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0171-9335
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
237-49
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pubmed:meshHeading |
pubmed-meshheading:18160177-Adenosine Triphosphate,
pubmed-meshheading:18160177-Amino Acid Sequence,
pubmed-meshheading:18160177-Animals,
pubmed-meshheading:18160177-Dictyostelium,
pubmed-meshheading:18160177-Escherichia coli,
pubmed-meshheading:18160177-Kinesin,
pubmed-meshheading:18160177-Microtubules,
pubmed-meshheading:18160177-Molecular Motor Proteins,
pubmed-meshheading:18160177-Molecular Sequence Data,
pubmed-meshheading:18160177-Phylogeny,
pubmed-meshheading:18160177-Protein Conformation,
pubmed-meshheading:18160177-Protein Structure, Tertiary,
pubmed-meshheading:18160177-Protozoan Proteins,
pubmed-meshheading:18160177-Recombinant Proteins,
pubmed-meshheading:18160177-Sequence Homology, Amino Acid
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pubmed:year |
2008
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pubmed:articleTitle |
Properties of the Kinesin-1 motor DdKif3 from Dictyostelium discoideum.
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pubmed:affiliation |
Department of Physics, Technical University Munich, James-Franck-Strasse, D-85748 Garching, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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