Structural and functional differences between mouse mot-1 and mot-2 proteins that differ in two amino acids.
Chaperone functions mediated by the heat-shock protein (HSP) family constitute a fundamental mechanism that governs the life span of organisms. Here we investigated the chaperone activities of the mitochondrial HSP70 protein, mortalin, which is a heat-uninducible stress protein involved in immortalization and tumorigenesis. There are two mortalin alleles, mot-1 and mot-2, in mouse, encoding two distinct proteins. Whereas an overexpression of mot-1-induced senescence in NIH 3T3 cells, overexpression of mot-2 promoted their malignant properties. Here, we provide evidence that mot-1 possesses very low chaperone activity as compared to mot-2. A "lazy lid" hypothesis is proposed for their differential aging phenotypes.
Deocaris
Custer C
CC
National Institute of Advanced Industrial Science & Technology (AIST), Tsukuba, Japan.
Yamasaki
Kazuhiko
K
Kaul
Sunil C
SC
Wadhwa
Renu
R
D000483:Alleles; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D045744:Cell Line, Tumor; D005347:Fibroblasts / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D008156:Luciferases / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D015394:Molecular Structure; D020673:Protein Renaturation; D014162:Transfection
D000596:Amino Acids; D018840:HSP70 Heat-Shock Proteins; C080352:mortalin; D008156:Luciferases