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- *******************************
- * Chaperonins cpn60 signature *
- *******************************
-
- Chaperonins [1,2] are proteins involved in the folding of proteins or the
- assembly of oligomeric protein complexes. Their role seems to be to assist
- other polypeptides to maintain or assume 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 cpn60 protein shows weak ATPase activity and is a highly conserved protein
- of about 550 to 580 amino acid residues which has been described by different
- names in different species:
-
- - Escherichia coli groEL protein, which is essential for the growth of the
- bacteria and the assembly of several bacteriophages.
- - Cyanobacterial groEL analogues.
- - Mycobacterium tuberculosis and leprae 65 Kd antigen, Coxiella burnetti heat
- shock protein B (gene htpB), Rickettsia tsutsugamushi major antigen 58, and
- Chlamydial 57 Kd hypersensitivity antigen (gene hypB).
- - Chloroplast RuBisCO subunit binding-protein alpha and beta chains, which
- bind ribulose bisphosphate carboxylase small and large subunits and are
- implicated in the assembly of the enzyme oligomer.
- - Mammalian mitochondrial matrix protein P1 (mitonin or P60).
- - Yeast HSP60 protein, a mitochondrial assembly factor.
-
- As a signature pattern for this protein, we have chosen a rather well
- conserved region of twelve residues, located in the last third of the cpn60
- sequence.
-
- -Consensus pattern: A-A-x-[EQ]-E-x(4)-G(3)
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Georgopoulos C.
- georgopo@cmu.unige.ch
-
- -Last update: October 1993 / Pattern and text revised.
-
- [ 1] Ellis R.J., van der Vies S.M.
- Annu. Rev. Biochem. 60:321-347(1991).
- [ 2] Zeilsta-Ryalls J., Fayet O., Georgopoulos C.
- Annu. Rev. Microbiol. 45:301-325(1991).
-