Chemical synthesis of 10 kDa chaperonin. Biological activity suggests chaperonins do not require other molecular chaperones.
Molecular chaperones are required for the correct folding and assembly of certain other polypeptides. It is not known whether molecular chaperones themselves require other chaperones to become functional. A 97-amino acid chaperone, the chaperonin 10 protein was chemically synthesised so that during synthesis and purification there was no contact of the chaperone with any other protein. The purified, synthetic chaperonin 10 protein formed oligomeric structures spontaneously and was biologically active as a chaperonin. This is the first description of a chemically synthesised chaperonin, and suggests that no other chaperones are required for correct folding, polymerisation and biological activity of this chaperone.
Department of Pharmaceutical Chemistry, School of Pharmacy, London, UK.
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Mascagni
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Tonolo
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Ball
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Lim
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Ellis
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Coates
D001426:Bacterial Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D018835:Chaperonin 10; D018833:Chaperonins; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D006360:Heat-Shock Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D007700:Kinetics; D011487:Protein Conformation; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry
D001426:Bacterial Proteins; D018835:Chaperonin 10; D006360:Heat-Shock Proteins; D011506:Proteins; D018833:Chaperonins; D012273:Ribulose-Bisphosphate Carboxylase