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Stalk region of kinesin-related protein Unc104 has moderate ability to form coiled-coil dimer.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Shimizu Y,Morii H,Arisaka F,Tanokura M

doi

10.1016/j.bbrc.2005.09.126

subject

Has Abstract

pub_date

2005-11-25 00:00:00

pages

868-74

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02162-5

journal_volume

337

pub_type

杂志文章

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