Ferritin from the spleen of the Anctartic teleost Trematomus bernacchii is an M-type homopolymer

• Published in: European Journal of Biochemistry
• Main Authors: MIGNOGNA, Giuseppina, CHIARALUCE, Roberta, CONSALVI, Valerio, CAVALLO, Stefano, STEFANINI, Simonetta, CHIANCONE, Emilia
• Other Authors: Mignogna, Giuseppina, Chiaraluce, Roberta, Consalvi, Valerio, Cavallo, Stefano, Stefanini, Simonetta, Chiancone, Emilia
• Format: Article in Journal/Newspaper
• Language: English
• Published: BLACKWELL PUBLISHING LTD, 9600 GARSINGTON RD, OXFORD OX4 2DG, OXON, ENGLAND 2002
• Subjects: Antarctic; The Antarctic; Antarc*
• Online Access: http://hdl.handle.net/11573/251998; https://doi.org/10.1046/j.1432-1327.2002.02762.x; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000174575200002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a; http://www.scopus.com/inward/record.url?eid=2-s2.0-0036231083&partnerID=65&md5=03fcce759764aa678281739a728344b3

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 ofmammalianL chains.Comparison of the amino-acid sequence with those available from lower vertebrates indicates that T. bernacchii ferritin can be classi®ed as an M-type homopolymer. Interestingly, the T. bernacchii ferritin chain shows 85.7% identity with a cold- inducible 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 signi®cant modi®cation of the protein stability. In fact, the stability of T. bernacchii ferritin to de- naturation induced by acid or temperature closely resembles that of mesophilic mammalian ferritins. Moreover iron is taken up e ciently and the activation energy of the reaction is 74.9 kJámol)1, a value slightly lower than that measured for the human recombinant H ferritin (80.8 kJámol)1).