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Vol. 8, Issue 12, 2693-2705, December 1997
and
*Structural Biology Laboratory and
As in many eukaryotic cells, fission yeast cytokinesis depends on
the assembly of an actin ring. We cloned
myp2+, a myosin-II in
Schizosaccharomyces pombe, conditionally required for
cytokinesis. myp2+, the second myosin-II
identified in S. pombe, does not completely overlap in
function with myo2+. The catalytic domain of
Myp2p is highly homologous to known myosin-IIs, and phylogenetic
analysis places Myp2p in the myosin-II family. The Myp2p sequence
contains well-conserved ATP- and actin-binding motifs, as well as two
IQ motifs. However, the tail sequence is unusual, since it is predicted
to form two long coiled-coils separated by a stretch of sequence
containing 19 prolines. Disruption of myp2+
is not lethal but under nutrient limiting conditions cells lacking myp2+ function are multiseptated, elongated,
and branched, indicative of a defect in cytokinesis. The presence of
salt enhances these morphological defects. Additionally,
Molecular Biology
and Virology Laboratory, The Salk Institute for Biological Studies, La
Jolla, California 92037
myp2 cells are cold sensitive in high salt, failing
to form colonies at 17°C. Thus, myp2+ is
required under conditions of stress, possibly linking extracellular growth conditions to efficient cytokinesis and cell growth. GFP-Myp2p localizes to a ring in the middle of late mitotic cells, consistent with a role in cytokinesis. Additionally, we constructed double mutants
of myp2 with temperature-sensitive mutant strains
defective in cytokinesis. We observed synthetic lethal interactions
between myp2 and three alleles of
cdc11ts, as well as more modest synthetic interactions
with cdc14ts and cdc16ts, implicating
myp2+ function for efficient cytokinesis
under normal conditions.
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