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Sro7p, a Saccharomyces cerevisiae Counterpart of the Tumor Suppressor l(2)gl Protein, Is Related to Myosins in Function
Mitsuhiro Kagamia, Akio Toh-ea, and Yasushi Matsuiaa Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113, Japan
Corresponding author: Yasushi Matsui, Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1, Hongo, Tokyo 113, Japan., matsui{at}biol.s.u-tokyo.ac.jp (E-mail).
Communicating editor: F. WINSTON
sro77
mutants showed a partial defect of organization of the polarized actin cytoskeleton and a cold-sensitive growth phenotype. A human counterpart of l(2)gl could suppress the sro7
sro77
defect. Similar to the l(2)gl protein, Sro7p formed a complex with Myo1p, a type II myosin. These results indicate that Sro7p and Sro77p are the yeast counterparts of the l(2)gl protein. Our genetic analysis revealed that deletion of SRO7 and SRO77 showed reciprocal suppression with deletion of MYO1 (i.e., the sro7
sro77
defect was suppressed by myo1
and vice versa). In addition, SRO7 showed genetic interactions with MYO2, encoding an essential type V myosin: Overexpression of SRO7 suppressed a defect in MYO2 and, conversely, overexpression of MYO2 suppressed the cold-sensitive phenotype of sro7
sro77
mutants. These results indicate that Sro7 function is closely related to both Myo1p and Myo2p. We propose a model in which Sro7 function is involved in the targeting of the myosin proteins to their intrinsic pathways.
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