Chaperonins [1,2] are proteins involved in the folding of proteins or the
assembly of oligomeric protein complexes. They seem to assist other
polypeptides in maintaining or assuming conformations which permit their
correct assembly into oligomeric structures. They are found in abundance in
prokaryotes, chloroplasts and mitochondria. Chaperonins form oligomeric
complexes and are composed of two different types of subunits: a 60 Kd
protein, known as cpn60 (groEL in bacteria) and a 10 Kd protein, known as
cpn10 (groES in bacteria).
The cpn10 protein binds to cpn60 in the presence of MgATP and suppresses the
ATPase activity of the latter. Cpn10 is a protein of about 100 amino acid
residues whose sequence is well conserved in bacteria, vertebrate mitochondria
and plants chloroplast [3,4]. Cpn10 assembles as an heptamer that forms a dome
. As a signature pattern for cpn10 we selected a region located in the N-terminal section of the protein.
This pattern is found twice in the plant chloroplast protein which
consist of the tandem repeat of a cpn10 domain.
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