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Vol. 12, Issue 4, 1161-1175, April 2001
We tested the ability of 87 profilin point mutations to complement
temperature-sensitive and null mutations of the single profilin gene of
the fission yeast Schizosaccharomyces pombe. We compared
the biochemical properties of 13 stable noncomplementing profilins with
an equal number of complementing profilin mutants. A large quantitative
database revealed the following: 1) in a profilin null background
fission yeast grow normally with profilin mutations having >10% of
wild-type affinity for actin or poly-L-proline, but lower
affinity for either ligand is incompatible with life; 2) in the
cdc3-124 profilin ts background, fission yeast function with profilin having only 2-5% wild-type affinity for actin or poly-L-proline; and 3) special mutations show that the
ability of profilin to catalyze nucleotide exchange by actin is an
essential function. Thus, poly-L-proline binding, actin
binding, and actin nucleotide exchange are each independent
requirements for profilin function in fission yeast.
Structural Biology Laboratory, The Salk Institute for
Biological Studies, La Jolla, California 92037; and *Graduate Program
in Cellular and Molecular Medicine, Johns Hopkins Medical School,
Baltimore, Maryland 21205
Corresponding author. E-mail address:
pollard{at}salk.edu.
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