Worm Breeder's Gazette 14(4): 24 (October 1, 1996)

These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

Expression of Klp-3, a Kinesin with a C-terminal motor, is in the pharynx and sphincter cells.

L. A. Khan, Z. K. Siddiqui, K. Nishikawa, S. S. Siddiqui

Lab. of Molecular Biology Toyohashi university of Technology Toyohashi 441, Japan.

We have characterized more than a dozen members of kinesin
superfamily of the motor proteins, based on the data and clones
obtained from sequencing project (Y. Kohara and Genomic consortium).
One of these, klp-3 has an unusual of the motor domain (which
is typically found in the N-terminus region), located in the
C-terminal region. Primary structure analysis shows that its
length is 598 aa, it contains consensus ATP and MT binding sites
at the C-terminal region. Secondary structure analysis indicates
that this protein contains three distinct regions, a C-terminal
globular motor domain, a coiled-coil rod and the tail which
is not globular like typical kinesins. In the C. elegans so
far there is only one C-terminal motor containing kinesin. To
see the expression, a klp-3::lacZ construct was made.
HindIII/BglII 3.5 kb fragment, containing about 1kb of the klp-3
promotor region, was put into the HindIII/BamHI site of the
vector pPD16.51. The klp-3::lacZ construct was coinjected with
the rol-6 marker DNA into the wild-type animals, the germ line
transformants were histochemically stained for the beta-galactosidase
activity. The staining is seen in pharynx, intestinal muscle and
in the rectal sphincter. In the pharynx it apparently expresses
in the mc1 and mc2 marginal cells (Leon Avery kindly helped us
in cell identification). Previously we have reported in the west
coast meeting abstract that the klp-3 (located on cosmid T09A5)
can rescue the him-14 mutant phenotype partially, i. e., the
number of males in the transformed progeny are reduced significantly.
Also, if the klp-3 gene is injected into the wild-type animals,
resulting transformants show sick worms, and about 5-10% males
in the progeny. Our two factor cross data places him-14 very
close to another kinesin gene unc-104, and thus it can not be
in the same region as T09A5. Thus, although Klp-3 is not encoded
by the him-14 gene, our results suggest that klp-3 and him-14
genes have some strong genetic interactions. Ken Kemphues and
Ann Villeneuve have cloned the him-14 gene by rescueing with
the cosmid ZK1127. We are interested to unravel the molecular
and genetic basis of these interactions.
We would like to thank the C. elegans genome sequencing consortium,
Leon Avery, Y. Kohara, Ken Kemphues, Ann Villeneuve, A. Fire,
M. Y. Ali, and the members of siddiqui Lab for their help.