Isolation and sequencing of the Candida albicans MSI3, a putative novel member of the HSP70 family.
We have reported previously that the expression of CGR1 increased at an early stage of the yeast-mycelial transition (morphogenesis) in Candida albicans. We now show that Cgr1p interacts in a yeast two-hybrid system with the C. albicans Msi3p (CaMsi3p), a putative novel member of the heat shock protein 70 (HSP70) family. The DNA sequence of CaMSI3 encodes a predicted protein of 702 amino acids with a molecular mass of 78.6 kDa. The amino acid sequence of CaMsi3p is 63% identical to Msi3p/Sse1p of the HSP70 family of Saccharomyces cerevisiae. Further, CaMSI3 complemented the temperature-sensitive phenotype of the msi3(-) mutant of S. cerevisiae. Other heat shock proteins of C. albicans are required for morphogenesis and are highly antigenic. These observations suggest that CaMSI3 may well provide functions for this organism unrelated to a heat shock function. The DDBJ Accession No. for the sequence reported in this paper is AB061274.
Cho
Tamaki
T
Department of Functional Bioscience, Fukuoka Dental College, Fukuoka 814-0193, Japan. chot 1@college.fdcnet.ac.jp
Toyoda
Mika
M
Sudoh
Masayuki
M
Nakashima
Yukihiko
Y
Calderone
Richard A
RA
Kaminishi
Hidenori
H
D000595:Amino Acid Sequence; D001483:Base Sequence; D002176:Candida albicans / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D004271:DNA, Fungal / Q000737:chemistry / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification*; D005816:Genetic Complementation Test; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010957:Plasmids; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D020798:Two-Hybrid System Techniques
D004271:DNA, Fungal; D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins