Sequence analysis of SLA2 of the dimorphic yeasts Candida albicans and Yarrowia 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 Y1Sla2p consist of 1063 and 1054 a a, respectively. The alignment of the deduced proteins of Saccharomyces cer evisiae, Y. lipolytica and C. albicans shows regions of identity in the N-t erminal 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 bo xes, displaying homology to the talin protein of mouse, Dictyostelium disco ideum, Caenorhabditis elegans and to human huntingtin interacting protein ( Hip Ip). The sequence data of C. albicans SLA2 are registered in the EMBL d atabase (AJ009556), and for the Y. lipolytica gene in GenBank (U65409). Cop yright (C) 1999 John Wiley & Sons, Ltd.