U. Lange et al., CLONING AND SEQUENCING OF A GENE CODING FOR AN ACTIN-BINDING PROTEIN OF SACCHAROMYCES-EXIGUUS, Biochimica et biophysica acta, N. Gene structure and expression, 1217(2), 1994, pp. 214-218
The actin binding protein Abp1p of the yeast Saccharomyces cerevisiae
is thought to be involved in the spatial organisation of cell surface
growth. It contains a potential actin binding domain and an SH-3 regio
n, a common motif of many signal transduction proteins [1]. We have cl
oned and sequenced an ABP1 homologous gene of Saccharomyces exiguus, a
yeast which is only distantly related to S. cerevisiae. The protein e
ncoded by this gene is slightly larger than the respective S. cerevisi
ae protein (617 versus 592 amino acids). The two genes are 67.4% ident
ical and the deduced amino acid sequences share an overall identity of
59.8%. The most conserved regions are the 148 N-terminal amino acids
containing the potential actin binding site and the 58 C-terminal amin
o acids including the SH3 domain. In addition, both proteins contain a
repeated motif of unknown function which is rich in glutamic acids wi
th the sequence EEEEEEEAPAPSLPSR in the S. exiguus Abp1p.