Cloning and sequencing of a gene coding for an actin binding protein of Saccharomyces exiguus.
The actin binding protein Abp1p of the yeast Saccharomyces cervisiae is thought to be involved in the spatial organisation of cell surface growth. It contains a potential actin binding domain and an SH-3 region, a common motif of many signal transduction proteins [1]. We have cloned and sequenced an ABP1 homologous gene of Saccharomyces exiguus, a yeast which is only distantly related to S. cerevisiae. The protein encoded by this gene is slightly larger than the respective S. cerevisiae protein (617 versus 592 amino acids). The two genes are 67.4% identical 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 amino acids including the SH3 domain. In addition, both proteins contain a repeated motif of unknown function which is rich in glutamic acids with the sequence EEEEEEEAPAPSLPSR in the S. exiguus Abp1p.
Lange
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U
Institut für Allgemeine Botanik und Pflanzenphysiologie, Universität Giessen, Germany.
Steiner
S
S
Grolig
F
F
Wagner
G
G
Philippsen
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P
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000235:genetics*; D008840:Microfilament Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D012440:Saccharomyces / Q000235:genetics*; D016415:Sequence Alignment
D000199:Actins; D002352:Carrier Proteins; C034037:F-actin-binding proteins; D005656:Fungal Proteins; D008840:Microfilament Proteins