Transcriptional inactivation of p53 by deletions and single amino acid changes in mouse mot-1 protein.
Mouse mortalin proteins, mot-1 and mot-2, differ by only two amino acid residues in their C-terminus. In previous studies we showed that they differ in their subcellular distributions and interactions with the tumor suppressor protein, p53. By using mot-1 deletion mutants and amino acid substitution constructs, we report here that inability of mot-1 to affect p53 activity in vivo is dependent on the presence of both of the unique mot-1 amino acids and all three of the predicted hsp70, EF hand, and leucine zipper motif regions. The two proteins and their single amino acid mutants showed different mobilities on SDS-polyacrylamide gel presenting an evidence for their different secondary structures. Taken together, the data suggest that each of the two differing amino acids between mot-1 and mot-2 is an important determinant of their secondary structures and in vivo activities.
Kaul
S C
SC
National Institute of Bioscience and Human Technology, AIST, 1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan.
Takano
S
S
Reddel
R R
RR
Mitsui
Y
Y
Wadhwa
R
R
D019943:Amino Acid Substitution; D000818:Animals; D002352:Carrier Proteins; D017930:Genes, Reporter; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics*; D051379:Mice; D018345:Mice, Knockout; D008822:Mice, Transgenic; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017384:Sequence Deletion; D014158:Transcription, Genetic; D014162:Transfection; D016159:Tumor Suppressor Protein p53 / Q000235:genetics* / Q000378:metabolism*
D002352:Carrier Proteins; D018840:HSP70 Heat-Shock Proteins; C083794:Hspa9 protein, mouse; C115087:Hspa9-ps1 protein, mouse; D016159:Tumor Suppressor Protein p53; C080352:mortalin