Sequence analysis ofSLA2 of the dimorphic yeastsCandida albicans andYarrowia lipolytica
Copyright policy )Sequence analysis ofSLA2 of the dimorphic yeastsCandida albicans andYarrowia lipolytica
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 degrees 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).
- University of Salamanca Spain
Saccharomyces cerevisiae Proteins, Base Sequence, Genes, Fungal, Molecular Sequence Data, Fungal Proteins, Cytoskeletal Proteins, Mice, Yeasts, Candida albicans, Animals, Humans, Amino Acid Sequence, Carrier Proteins
Saccharomyces cerevisiae Proteins, Base Sequence, Genes, Fungal, Molecular Sequence Data, Fungal Proteins, Cytoskeletal Proteins, Mice, Yeasts, Candida albicans, Animals, Humans, Amino Acid Sequence, Carrier Proteins
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