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J Biol Chem, Vol. 273, Issue 19, 11852-11861, May 8, 1998
From the Departments of Pharmacology and Cancer Biology and of
Biochemistry, Duke Medical Center,
Durham, North Carolina 27710
Sequence analysis of Saccharomyces
cerevisiae chromosome IX identified a 946 amino acid open reading
frame (YIL002C), designated here as INP51, that has
carboxyl- and amino-terminal regions similar to mammalian inositol
polyphosphate 5-phosphatases and to yeast SAC1. This
two-domain primary structure resembles the mammalian 5-phosphatase,
synaptojanin. We report that Inp51p is associated with a particulate
fraction and that recombinant Inp51p exhibits intrinsic
phosphatidylinositol 4,5-bisphosphate 5-phosphatase activity. Deletion
of INP51 (inp51) results in a
"cold-tolerant" phenotype, enabling significantly faster growth at
temperatures below 15 °C as compared with a parental strain.
Complementation analysis of an inp51 mutant strain
demonstrates that the cold tolerance is strictly due to loss of
5-phosphatase catalytic activity. Furthermore, deletion of
PLC1 in an inp51 mutant does not abrogate cold
tolerance, indicating that Plc1p-mediated production of soluble inositol phosphates is not required. Cells lacking INP51
have a 2-4-fold increase in levels of phosphatidylinositol
4,5-bisphosphate and inositol 1,4,5-trisphosphate, whereas cells
overexpressing Inp51p exhibit a 35% decrease in levels of
phosphatidylinositol 4,5-bisphosphate. We conclude that
INP51 function is critical for proper phosphatidylinositol
4,5-bisphosphate homeostasis. In addition, we define a novel role for a
5-phosphatase loss of function mutant that improves the growth of cells
at colder temperatures without alteration of growth at normal
temperatures, which may have useful commercial applications.
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