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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have isolated a 1224 bp cDNA clone from a Bombyx mori embryonic cDNA library which contains sequences homologous to the kinesin-like protein gene, ncd, which is required for distribution of chromosomes at meiosis in Drosophila melanogaster females. This clone includes both a microtubule motor and the ATP-binding domains found in kinesin-like proteins. The motor domain is classified in the group of the BimC and cut7, which have a role in spindle formation during mitosis of Aspergillus nidulans and Schizosaccharomyces pombe, respectively. However, the location of the domain at the carboxy terminus is not common in this family, except for ncd and KAR3.
Insect Mol Biol 1994 Nov
PMID:cDNA structure and characterization of a kinesin-like protein from the silkworm Bombyx mori. 770 3

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.
J Mol Biol 1995 Mar 31
PMID:Exclusive expression of C. elegans osm-3 kinesin gene in chemosensory neurons open to the external environment. 771 94

We report that the human gene SB1.8 (DXS423E) encodes a protein of 1233 amino acids that is highly homologous (30% identity) to the essential yeast protein SMC1 which is required for the segregation of chromosomes at mitosis. Both SB1.8 and SMC1 contain an N-terminal NTP binding site, a central coiled-coil region and a C-terminal helix-loop-helix domain, and have structural features in common with the force generating proteins myosin and kinesin. SB1.8 also exhibits regions of homology and overall structural similarity to the prokaryote (Mycoplasma hyorhinis) protein 115p. Thus SB1.8 and SMC1 are members of a highly conserved and ubiquitous family of proteins that appear to have a fundamental role in cell division. In addition we show that SB1.8 (DXS423E) maps to a cosmid contig that lies centromeric to the OATL2 locus at chromosome Xp11.2.
Hum Mol Genet 1995 Feb
PMID:The human SB1.8 gene (DXS423E) encodes a putative chromosome segregation protein conserved in lower eukaryotes and prokaryotes. 775 74

We have identified a human cDNA that is homologous to the chicken kinectin, a putative receptor for the organelle motor kinesin. The human cDNA clone hybridized to a single 4.6-kb mRNA species that codes for a protein of 156 kDa molecular mass. The predicted primary translation product contains an N-terminal transmembrane helix followed by a bipartite nuclear localization sequence and two further C-terminal leucine zipper motifs. In addition, the aminoacid sequence revealed a large region (327-1362) of predicted alpha-helical coiled coils. A monoclonal antibody CT-1 raised against a GST-kinectin fusion protein produced a perinuclear, endoplasmic reticulum-like staining pattern in diverse cell types from different species, indicating evolutionary conservation. Monoclonal antibody CT-1 and anti-chicken kinectin antibodies cross-reacted both in Western blotting and immunoprecipitation with a 160-kDa protein, confirming the antigenic identity of this 160-kDa protein with chicken kinectin. Epitope tagging studies revealed that the nuclear localization sequence motif of kinectin is not functional. Furthermore, a truncated kinesin cDNA lacking the N-terminal hydrophobic domain revealed a nonspecific cytoplasmic staining pattern. Together the data suggest that kinectin is an integral membrane protein anchored in the endoplasmic reticulum via a transmembrane domain.
Mol Biol Cell 1995 Feb
PMID:Molecular cloning and characterization of human kinectin. 778 43

Kinectin is a kinesin-binding protein (Toyoshima et al., 1992) that is required for kinesin-based motility (Kumar et al., 1995). A kinectin cDNA clone containing a 4.7-kilobase insert was isolated from an embryonic chick brain cDNA library by immunoscreening with a panel of monoclonal antibodies. The cDNA contained an open reading frame of 1364 amino acids encoding a protein of 156 kDa. A bacterially expressed product of the full length cDNA bound purified kinesin. Transient expression in CV-1 cells gave an endoplasmic reticulum distribution that depended upon the N-terminal domain. Analysis of the predicted amino acid sequence indicated a highly hydrophobic near N-terminal stretch of 28 amino acids and a large portion (326-1248) of predicted alpha helical coiled coils. The 30-kDa fragment containing the N-terminal hydrophobic region was produced by cell-free in vitro translation and found to assemble with canine pancreas rough microsomes. Cleavage of the N terminus was not observed confirming its role as a potential transmembrane domain. Thus, the kinectin cDNA encodes a cytoplasmic-oriented integral membrane protein that binds kinesin and is likely to be a coiled-coil dimer.
Mol Biol Cell 1995 Feb
PMID:Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysis. 778 44

We investigated the mechanism of poleward microtubule flux in the mitotic spindle by generating spindle subassemblies in Xenopus egg extracts in vitro and assaying their ability to flux by photoactivation of fluorescence and low-light multichannel fluorescence video-microscopy. We find that monopolar intermediates of in vitro spindle assembly (half-spindles) exhibit normal poleward flux, as do astral microtubule arrays induced by the addition of dimethyl sulfoxide to egg extracts in the absence of both chromosomes and conventional centrosomes. Immunodepletion of the kinesin-related microtubule motor protein Eg5, a candidate flux motor, suggests that Eg5 is not required for flux. These results suggest that poleward flux is a basic element of microtubule behavior exhibited by even simple self-organized microtubule arrays and presumably underlies the most elementary levels of spindle morphogenesis.
Mol Biol Cell 1994 Feb
PMID:Microtubule flux in mitosis is independent of chromosomes, centrosomes, and antiparallel microtubules. 801 7

Complementary DNAs of two kinesin-related genes, katB and katC, were isolated from Arabidopsis thaliana and sequenced. The carboxyl-terminal regions of the polypeptides encoded by these genes, especially the presumptive ATP-binding and microtubule-binding domains, share significant sequence homology with the mechanochemical motor domain of the kinesin heavy chain. The predicted secondary structures of KatB and KatC proteins include a large globular domain in the carboxyl-terminal region and a small globular domain in the amino-terminal region that are separated by a long alpha-helical coiled-coil with heptad repeats. A truncated KatC polypeptide (KatC(207-754)), which includes the carboxyl-terminal region of KatC, was expressed in Escherichia coli and was shown to possess microtubule-stimulated ATPase activity and to bind to microtubules in an ATP-sensitive manner, both of which are characteristics of kinesin and kinesin-like proteins.
Plant Mol Biol 1994 Aug
PMID:Sequencing and characterization of the kinesin-related genes katB and katC of Arabidopsis thaliana. 807 2

We have analyzed a collection of 12 mutations in the Drosophila melanogaster nod locus, which encodes a kinesin-like protein involved in female meiotic chromosome segregation. The kinesin-like domain is at the N-terminus of the protein, while the C-terminal portion of the protein is unique. Four of the mutations are missense and affect highly conserved domains of the kinesin-like portion of the predicted protein, and thus demonstrate that the sequence conservation is biologically relevant. Surprisingly, two other mutations, which behave genetically as null alleles, are the result of mutations in the last exon of the nod gene. Thus, these two mutations affect the most C-terminal residues in the unique portion of the predicted protein. Based on these mutations, we suggest that this part of the protein may also be essential for wild-type function. The mutations were induced by either gamma-rays or ethyl methanesulfonate (EMS). All of the gamma-ray induced mutations were small or large chromosomal rearrangements, while all of the EMS mutations were G-->A transitions. These findings are consistent with the biochemical basis of the mode of action of each mutagen.
Mol Gen Genet 1994 Jan
PMID:A structure-function analysis of NOD, a kinesin-like protein from Drosophila melanogaster. 815 64

We have demonstrated the presence of kinesin in the secretory pancreatic tissue using SDS-PAGE, immunoblot and immunoelectron microscopy techniques. Polyclonal antibodies were raised against the rat brain kinesin heavy chain and affinity-purified. Immunoblot studies showed that these antibodies were bound to a 116 kDa protein found in rat pancreas crude extracts and in partially purified kinesin fractions. Kinesin identification was also performed by a cosedimentation procedure based on its strong binding to microtubules in the presence of sodium fluoride. The microtubule-kinesin complex was observed by immunoelectron microscopy gold staining. The reversible association of kinesin with microtubules was generated by MgATP.
Cell Mol Biol (Noisy-le-grand) 1993 May
PMID:Rat pancreas kinesin: identification and potential binding to microtubules. 833 81

A gene family, designated kat, has been characterized in Arabidopsis thaliana by genomic Southern hybridization and nucleotide sequencing analysis. The kat gene family includes at least five members, named katA, katB, katC, katD and katE, whose products share appreciable sequence similarities in their presumptive ATP-binding and microtubule-binding motifs with known kinesin-like proteins. The carboxyl-terminal region of the KatA protein deduced from the nucleotide sequence of the cDNA clone has considerable homology with the mechanochemical motor domain of the kinesin heavy chain. The predicted secondary structure of the KatA protein indicates two globular domains separated by a long alpha helical coiled coil with heptad repeat structures, such as are commonly found in kinesin-like proteins.
Mol Gen Genet 1993 Apr
PMID:Identification of a gene family (kat) encoding kinesin-like proteins in Arabidopsis thaliana and the characterization of secondary structure of KatA. 849 4


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