Sequence analysis of SLA2 of the dimorphic yeasts Candida albicans and Yarrowia lipolytica

• Published in: Yeast (Chichester, England) England), 1999-10, Vol.15 (14), p.1519-1528
• Main Authors: Melms, Anne‐Sophie, Gausmann, Ulrike, Swoboda, Rolf K., Dominguez, Angel, Kurischko, Cornelia
• Format: Article
• Language: English
• Subjects: actin binding protein; Amino Acid Sequence; Animals; Base Sequence; Candida albicans; Candida albicans - genetics; Carrier Proteins - chemistry; Carrier Proteins - genetics; Cytoskeletal Proteins; dimorphic yeast; Fungal Proteins - chemistry; Fungal Proteins - genetics; Genes, Fungal; Hip1 protein; Humans; Mice; Molecular Sequence Data; Saccharomyces cerevisiae Proteins; SLA2; SLA2 gene; Sla2 protein; Yarrowia lipolytica; Yeasts - genetics
• ISSN: 0749-503X; 1097-0061
• DOI: 10.1002/(SICI)1097-0061(199910)15:14<1519::AID-YEA475>3.0.CO;2-2

We report the complete nucleotide sequence of SLA2 of the dimorphic yeasts Candida albicans and Yarrowia lipolytica. In Saccharomyces cerevisiae, SLA2 codes for an actin binding protein. The deduced amino acid (aa) sequences of C. albicans CaSla2p and Y. lipolytica YlSla2p consist of 1063 and 1054 aa, respectively. The alignment of the deduced proteins of Saccharomyces cerevisiae, Y. lipolytica and C. albicans shows regions of identity in the N‐terminal part of the proteins, which are essential for growth at 37°C, endocytosis and actin organization in S. cerevisiae. The Sla2p proteins have also several conserved regions in the C‐terminal moiety, the I/LWEQ boxes, displaying homology to the talin protein of mouse, Dictyostelium discoideum, Caenorhabditis elegans and to human huntingtin interacting protein (Hip 1p). The sequence data of C. albicans SLA2 are registered in the EMBL database (AJ009556), and for the Y. lipolytica gene in GenBank (U65409). Copyright © 1999 John Wiley & Sons, Ltd.