Linked Life Data

16214110

Source:http://linkedlifedata.com/resource/pubmed/id/16214110

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-10-21
pubmed:abstractText
Unc104/KIF1A, a kinesin family member, is reported to be monomeric in solution, though its polypeptide has regions that potentially form coiled coils. For a better understanding of the mechanism underlying Unc104/KIF1A's motility, it is important to evaluate the dimerization ability of this protein. The CD measurement of relevant segments of Caenorhabditis elegans Unc104 indicated that peptides having a common region (N358-K379) showed spectra characteristic to an alpha-helix. Dimerization by coiled-coil formation was confirmed by analytical ultracentrifugation. By analyzing the concentration dependence of the CD spectra, the monomer-dimer dissociation constant, Kd, of (N354-E388) was estimated to be about 5 microM, which is considerably larger than that of the corresponding segment of human kinesin (62 nM). Though its dimerization ability is rather moderate, Unc104/KIF1A could nonetheless dimerize and therefore could move by the same mechanism as human kinesin when the concentration of Unc104 is high due to, e.g., local crowding. This suggests that the motility could be controlled by the concentration of the motor protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
337
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
868-74
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Stalk region of kinesin-related protein Unc104 has moderate ability to form coiled-coil dimer.
pubmed:affiliation
Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
pubmed:publicationType
Journal Article