Yeast TOR (DRR) proteins: amino-acid sequence alignment and identification of structural motifs

• Published in: Gene Vol. 141; no. 1; pp. 133 - 136
• Main Authors: Cafferkey, Robert, McLaughlin, Megan M, Young, Peter R, Johnson, Randall K, Livi, George P
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 08.04.1994
• Subjects: Alleles; Amino Acid Sequence; amino acid sequences; Base Sequence; binding proteins; Cell Cycle Proteins; drug resistance; FKBP12; Fungal Proteins - chemistry; Fungal Proteins - genetics; Genes, Fungal - genetics; immuniphilins; immunophilins; immunosuppressive agents; interactions; Molecular Sequence Data; mutation; nuclear localization signals; Phosphatidylinositol 3-Kinases; Phosphotransferases (Alcohol Group Acceptor) - chemistry; Phosphotransferases (Alcohol Group Acceptor) - genetics; Point Mutation - genetics; Rapamycin; Saccharomyces cerevisiae; Saccharomyces cerevisiae - chemistry; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; aa; nt; FKBP12; Rapamycin; nuclear localization signals; TORI and TOR2; immunophilins; bp; R; DRR1 and DRR2; TOR1 and TOR2; PI; oligo; Rm; Saccharomyces cerevisiae; wt; PCR
• ISSN: 0378-1119; 1879-0038
• DOI: 10.1016/0378-1119(94)90141-4

The yeast TORI (DRR1) and TOR2 (DRR2) proteins are putative targets of the immunosuppressive drug rapamycin (Rm), denned by dominant drug-resistance mutations. They share a large C-terminal domain that exhibits sequence similarity to the 110-kDa subunit of phosphatidylinositol (PI) 3-kinases. In this report, we present an amino acid (aa) sequence alignment of TORI (DRR1) and TOR2 (DRR2) and identify conserved and nonconserved motifs within the N-terminal domain that are indicative of possible nuclear localization. We also show that the mutations responsible for Rm resistance in four independent drr2 dom alleles alter the identical aa (Ser 1975→ Arg) previously identified in drr 1 dom mutants (Ser 1972→ Arg or Asn). Models for TOR (DRR) protein function are discussed.