TAILIEUCHUNG - Báo cáo Y học: Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is an M-type homopolymer

Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is composed of a single subunit that contains both the ferroxidase center residues, typical of mammalian H chains, and the carboxylate residues forming the micelle nucleation site, typical of mammalian L chains. Comparison of the amino-acid sequence with those available from lower vertebrates indicates that T. bernacchii ferritin can be classified as an M-type homopolymer. Interestingly, the T. bernacchii ferritin chain shows identity with a coldinducible ferritin chain of the rainbow trout Salmo gairdneri | Eur. J. Biochem. 269 1600-1606 2002 FEBS 2002 Ferritin from the spleen of the Antarctic teleost Trematomusbernacchii is an M-type homopolymer Guiseooina Mianoana1 Roberta Chiaraluce1 Valerio Consalvi1 Stefano Cavallo1 Simonetta Stefanini1 and Emilia Chiancone1 2 1 Department of Biochemical Sciences and 2CNR Center of Molecular Biology Department of Biochemical Sciences A. Rossi Fanelli University of Rome La Sapienza Italy Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is composed of a single subunit that contains both the ferroxidase center residues typical of mammalian H chains and the carboxylate residues forming the micelle nucleation site typical of mammalian L chains. Comparison of the amino-acid sequence with those available from lower vertebrates indicates that T. bernacchii ferritin can be classihed as an M-type homopolymer. Interestingly the T. bernacchii ferritin chain shows identity with a coldinducible ferritin chain of the rainbow trout Salmo gairdneri. The structural and functional properties indicate that cold acclimation and functional adaptation to low temperatures are achieved without signihcant modihcation of the protein stability. In fact the stability of T. bernacchii ferritin to denaturation induced by acid or temperature closely resembles that of mesophilic mammalian ferritins. Moreover iron is taken up efficiently and the activation energy of the reaction is kJ-mol-1 a value slightly lower than that measured for the human recombinant H ferritin kJ-mol-1 . Keywords amino-acid sequence cold adaptation iron incorporation stability Trematomus bernachii Antarctic hsh ferritin. Several molecular adaptation mechanisms have been developed by living organisms under extreme environmental conditions 1 . In many cases cold adaptation is achieved by modihcation of the structural and functional properties of proteins 2 . It follows that the correlation between the physicochemical properties of proteins and cold .

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