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Vol. 11, Issue 1, 79-91, January 2000
and
*Biochemistry Cellular and Molecular Biology Graduate Program,
Johns Hopkins University School of Medicine, Baltimore, Maryland 21205;
and Schizosaccharomyces pombe has two myosin-IIs, Myo2p
and Myp2p, which both concentrate in the cleavage furrow during
cytokinesis. We studied the phenotype of mutant myosin-II strains to
examine whether these myosins have overlapping functions in the cell. myo2+ is essential.
myp2+ cannot rescue loss of
myo2+ even at elevated levels of expression.
myp2+ is required under specific nutritional
conditions; thus myo2+ cannot rescue under
these conditions. Studies with chimeras show that the tails rather than
the structurally similar heads determine the gene-specific functions of
myp2+ and myo2+. The
Myo2p tail is a rod-shaped coiled-coil dimer that aggregates in low
salt like other myosin-II tails. The Myp2p tail is monomeric in high
salt and is insoluble in low salt. Biophysical properties of the
full-length Myp2p tail and smaller subdomains indicate that two
predicted coiled-coil regions fold back on themselves to form a
rod-shaped antiparallel coiled coil. This suggests that Myp2p is the
first type II myosin with only one head. The C-terminal two-thirds of
Myp2p tail are essential for function in vivo and may interact with
components of the salt response pathway.
Structural Biology Laboratory, The Salk Institute for
Biological Studies, La Jolla, California 92037
Corresponding author. E-mail address:
pollard{at}salk.edu.
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