The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi.
Ferritins from the liver and spleen of the cold-adapted Antarctic teleosts Trematomus bernacchii and Trematomus newnesi have been isolated and characterized. Interestingly, only H- and M-chains are expressed and no L-chains. The H-chains contain the conserved ferroxidase center residues while M-chains harbor both the ferroxidase center and the micelle nucleation site ligands. Ferritins have an organ-specific subunit composition, they are: M homopolymers in spleen and H/M heteropolymers in liver. The M-chain homopolymer mineralizes iron at higher rate with respect to the H/M heteropolymer, which however is endowed with a lower activation energy for the iron incorporation process, indicative of a higher local flexibility. These findings and available literature data on ferritin expression in fish point to the role of tissue-specific expression of different chains in modulating the iron oxidation/mineralization process.
Giorgi
Alessandra
A
Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza, Università di Roma, P.le A. Moro, 5, 00185 Roma, Italy.
Mignogna
Giuseppina
G
Bellapadrona
Giuliano
G
Gattoni
Maurizio
M
Chiaraluce
Roberta
R
Consalvi
Valerio
V
Chiancone
Emilia
E
Stefanini
Simonetta
S
D000818:Animals; D005293:Ferritins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D007501:Iron / Q000737:chemistry; D008024:Ligands; D008099:Liver / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D010473:Perciformes; D011108:Polymers / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013154:Spleen / Q000378:metabolism; D013696:Temperature
D008024:Ligands; D010455:Peptides; D011108:Polymers; D005293:Ferritins; D007501:Iron