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An actin point‐mutation neighboring the ‘hydrophobic plug’ causes defects in the maintenance of cell polaroty and septum organization in the fission yeast Schizosaccharomyces pombe
Author(s) -
Ishiguro Junpei,
Kobayashi Wataru
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00819-8
Subject(s) - schizosaccharomyces pombe , schizosaccharomyces , fission , yeast , microbiology and biotechnology , saccharomyces cerevisiae , biology , chemistry , genetics , physics , quantum mechanics , neutron
The fission yeast cps8 mutation gives rise to abnormally enlarged and dispolarized cells, each of which contains several nuclei with aberrant multisepta. Molecular cloning and sequence analysis of the cps8 gene indicated that it encodes an actin with an amino acid substitution of aspartic acid for glycine at residue 273 in the hydrophobic loop that is located between actin subdomains 3 and 4. Fluorescence microscopy using phalloidin and anti‐actin antibody revealed changes in the F‐actin structure and distribution in the mutant cells. These results indicate that the hydrophobic loop plays an essential role for creating normal F‐actin structure, only by which cell polarity and the late mitotic events can be maintained properly.