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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
1998-2-27
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pubmed:databankReference |
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pubmed:abstractText |
We cloned the myo3+ gene of Schizosaccharomyces pombe which encodes a type-II myosin heavy chain. myo3 null cells showed a defect in cytokinesis under certain conditions. Overproduction of Myo3 also showed a defect in cytokinesis. Double mutant analysis indicated that Myo3 genetically interacts with Cdc8 tropomyosin and actin. Myo3 may be implicated in cytokinesis and stabilization of F-actin cables. Moreover, the function of Myo2 can be replaced by overexpressed Myo3. We observed a modest synthetic interaction between Myo2 and Myo3. Thus, Myo2 and Myo3 seem to cooperate in the formation of the F-actin ring in S. pombe.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MYO2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MYO2 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type V,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tropomyosin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
420
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9459302-Actins,
pubmed-meshheading:9459302-Amino Acid Sequence,
pubmed-meshheading:9459302-Bacterial Proteins,
pubmed-meshheading:9459302-Blotting, Southern,
pubmed-meshheading:9459302-Carrier Proteins,
pubmed-meshheading:9459302-Cell Division,
pubmed-meshheading:9459302-Cell Nucleus,
pubmed-meshheading:9459302-Cloning, Molecular,
pubmed-meshheading:9459302-Fluorescent Dyes,
pubmed-meshheading:9459302-Fungal Proteins,
pubmed-meshheading:9459302-Gene Expression Regulation, Fungal,
pubmed-meshheading:9459302-Microscopy, Fluorescence,
pubmed-meshheading:9459302-Molecular Sequence Data,
pubmed-meshheading:9459302-Myosin Heavy Chains,
pubmed-meshheading:9459302-Myosin Type II,
pubmed-meshheading:9459302-Myosin Type V,
pubmed-meshheading:9459302-Myosins,
pubmed-meshheading:9459302-Phenotype,
pubmed-meshheading:9459302-Restriction Mapping,
pubmed-meshheading:9459302-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9459302-Schizosaccharomyces,
pubmed-meshheading:9459302-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:9459302-Sequence Analysis, DNA,
pubmed-meshheading:9459302-Tropomyosin
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pubmed:year |
1997
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pubmed:articleTitle |
Identification of Myo3, a second type-II myosin heavy chain in the fission yeast Schizosaccharomyces pombe.
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pubmed:affiliation |
Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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