Yeast TOR (DRR) proteins: amino-acid sequence alignment and identification of structural motifs.
The yeast TOR1 (DRR1) and TOR2 (DRR2) proteins are putative targets of the immunosuppressive drug rapamycin (Rm), defined 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 TOR1 (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 drr2dom alleles alter the identical aa (Ser1975-->Arg) previously identified in drr1dom mutants (Ser1972-->Arg or Asn). Models for TOR (DRR) protein function are discussed.
Cafferkey
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Department of Biomolecular Discovery, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406.
McLaughlin
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Young
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PR
Johnson
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RK
Livi
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GP
D000483:Alleles; D000595:Amino Acid Sequence; D001483:Base Sequence; D018797:Cell Cycle Proteins; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D005800:Genes, Fungal / Q000235:genetics; D008969:Molecular Sequence Data; D019869:Phosphatidylinositol 3-Kinases; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000235:genetics; D017354:Point Mutation / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D018797:Cell Cycle Proteins; D005656:Fungal Proteins; D019869:Phosphatidylinositol 3-Kinases; D017853:Phosphotransferases (Alcohol Group Acceptor); D029701:Saccharomyces cerevisiae Proteins; C083324:TOR1 protein, S cerevisiae; C081135:TOR2 protein, S cerevisiae