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J Biol Chem, Vol. 273, Issue 45, 29586-29591, November 6, 1998
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From the The mortalin genes, mot-1 and
mot-2, are hsp70 family members that were originally cloned
from normal and immortal murine cells, respectively. Their proteins
differ by only two amino acid residues but exhibit different
subcellular localizations, arise from two distinct genes, and have
contrasting biological activities. We report here that the two proteins
also differ in their interactions with the tumor suppressor protein
p53. The pancytosolic mot-1 protein in normal cells did not show
colocalization with p53; in contrast, nonpancytosolic mot-2 and p53
overlapped significantly in immortal cells. Transfection of
mot-2 but not mot-1 resulted in the repression
of p53-mediated transactivation in p53-responsive reporter assays.
Inactivation of p53 by mot-2 was supported by the down-regulation of
p53-responsive genes p21WAF-1 and
mdm-2 in mot-2-transfected cells only.
Furthermore, NIH 3T3 cells transfected with expression plasmid encoding
green fluorescent protein-tagged
mot-2 but not mot-1 showed an abrogation of
nuclear translocation of wild-type p53. These results demonstrate a
novel mechanism of p53 inactivation by mot-2 protein.
Chugai Research Institute for Molecular
Medicine, 153-2 Nagai, Niihari, Ibaraki 300-41, Japan, the
¶ National Institute of Bioscience and Human Technology, AIST, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan, and the Children's
Medical Research Institute, 214 Hawkesbury Road, Westmead Sydney, New
South Wales 2145, Australia
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