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Vol. 10, Issue 12, 4341-4353, December 1999
*Department of Biology, Washington University, St. Louis, Missouri
63130; and We have identified partial loss of function mutations in class VI
unconventional myosin, 95F myosin, which results in male sterility.
During spermatogenesis the germ line precursor cells undergo mitosis
and meiosis to form a bundle of 64 spermatids. The spermatids remain
interconnected by cytoplasmic bridges until individualization. The
process of individualization involves the formation of a complex of
cytoskeletal proteins and membrane, the individualization complex (IC),
around the spermatid nuclei. This complex traverses the length of each
spermatid resolving the shared membrane into a single membrane
enclosing each spermatid. We have determined that 95F
myosin is a component of the IC whose function is essential for
individualization. In wild-type testes, 95F myosin localizes to the
leading edge of the IC. Two independent mutations in 95F myosin reduce
the amount of 95F myosin in only a subset of tissues, including the
testes. This reduction of 95F myosin causes male sterility as a result
of defects in spermatid individualization. Germ line transformation
with the 95F myosin heavy chain cDNA rescues the male sterility
phenotype. IC movement is aberrant in these 95F myosin mutants,
indicating a critical role for 95F myosin in IC movement. This report
is the first identification of a component of the IC other than actin.
We propose that 95F myosin is a motor that participates in membrane
reorganization during individualization.
University of Edinburgh, Institute of Cell and
Molecular Biology, Edinburgh EH9 3JR, United Kingdom
Present address: J579, HSB, Department of
Biochemistry, Box 357350, University of Washington, Seattle, WA 98195.
§
Corresponding author. E-mail address:
miller{at}biology.wustl.edu.
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