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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1995-5-15
|
| pubmed:databankReference | |
| pubmed:abstractText |
In Caenorhabditis elegans three genetic loci osm-3, unc-104 and unc-116 have been identified, which encode anterograde motor kinesin. Here we show that osm-3 encodes a 672 amino acid long kinesin-like protein (KLP) that contains all three functional domains similar to the kinesin heavy chain, including a globular motor region, an alpha-helical coiled-coil rod, and a globular tail region. OSM-3 shows homology in both the motor and rod domains with kinesins from divergent species such as mouse KIF3, and sea urchin KRP95, and also with the rod domains of several non-kinesin proteins, such as myosin, ezrin, outer membrane proteins alpha precursor OMPA, yeast intracellular protein transport USO1, and the rat neurofilament NF-H. Temporal and spatial expression of the osm-3::lacZ fusion gene during development is limited to an exclusive set of 26 chemosensory neurons whose dendritic endings are exposed to the external environment, including six IL2 neurons of the inner labial sensilla, eight pairs of amphid neurons (ADF, ADL, ASE, ASG, ASH, ASI, ASJ, ASK) in the head, and two pairs of phasmid neurons (PHA and PHB) in the tail. Our data are consistent with the known structural defects in the amphid and phasmid sensilla in osm-3 mutants and also show the expression of the gene in IL2 neurons. Temporally, the gene is differentially expressed in all three types of chemosensory sensilla. Further work on osm-3, unc-104 and unc-116 mutants should give insight into the in vivo functions of the kinesin family during C. elegans neurogenesis.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Kinesin,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
31
|
| pubmed:volume |
247
|
| pubmed:geneSymbol |
osm-3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
377-89
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:7714894-Amino Acid Sequence,
pubmed-meshheading:7714894-Animals,
pubmed-meshheading:7714894-Base Sequence,
pubmed-meshheading:7714894-Caenorhabditis elegans,
pubmed-meshheading:7714894-Caenorhabditis elegans Proteins,
pubmed-meshheading:7714894-Chemoreceptor Cells,
pubmed-meshheading:7714894-Enzyme Induction,
pubmed-meshheading:7714894-Gene Expression Regulation, Developmental,
pubmed-meshheading:7714894-Genes, Helminth,
pubmed-meshheading:7714894-Helminth Proteins,
pubmed-meshheading:7714894-Kinesin,
pubmed-meshheading:7714894-Molecular Sequence Data,
pubmed-meshheading:7714894-Nerve Tissue Proteins,
pubmed-meshheading:7714894-Neurons, Afferent,
pubmed-meshheading:7714894-Protein Structure, Tertiary,
pubmed-meshheading:7714894-Recombinant Fusion Proteins,
pubmed-meshheading:7714894-Sequence Alignment,
pubmed-meshheading:7714894-Sequence Homology
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Exclusive expression of C. elegans osm-3 kinesin gene in chemosensory neurons open to the external environment.
|
| pubmed:affiliation |
Dept of Ecological Engineering, Toyohashi University of Technology, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|