The complete primary structure of rat chaperonin 10 reveals a putative beta alpha beta nucleotide-binding domain with homology to p21ras.
The first complete amino-acid sequence of a mitochondrial chaperonin 10 is reported. The amino-terminal alanine residue is acetylated, a modification that may be required for the interaction with heptameric chaperonin 60. Part of the sequence constitutes a potential dinucleotide binding motif and is identical with 7 out of 10 residues in the GTP-binding site of p21ras. This similarity may be the structural basis for the recently discovered complex between p21ras and chaperonin 60 in intact cells (Ikawa, S. and Weinberg, R.A. (1992) Proc. Natl. Acad. Sci. USA 89, 2012-2016).
Hartman
D J
DJ
Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Hoogenraad
N J
NJ
Condron
R
R
Høj
P B
PB
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins / Q000737:chemistry*; D007770:L-Lactate Dehydrogenase / Q000737:chemistry; D008969:Molecular Sequence Data; D015689:Oncogene Protein p21(ras) / Q000737:chemistry*; D051381:Rats; D016415:Sequence Alignment
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D007770:L-Lactate Dehydrogenase; D015689:Oncogene Protein p21(ras)