Archaebacterial chaperonin-mediated protein stabilization

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

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530412, 530427, 530820, 530402, 435 691, 536 237, C07K 106

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054281318

ABSTRACT:
TF55 is a homooligomeric complex of two stacked rings, closely resembling the quaternary structure of the chaperonins, groEL, hsp60, and RUBISCO-binding protein. Most rings of TF55 contain 9 radially arranged members. The TF55 complex binds unfolded polypeptides in vitro, preventing aggregation at elevated temperature, and exhibits ATPase activity, features consistent with its function as a molecular chaperone. At the level of primary structure, TF55 is not significantly related to the chaperonins but is highly homologous (36-40% identity) to a ubiquitous eukaryotic protein, t complex polypeptide 1 (PCT1).

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