Mitochondrial ferritin

Short description: Protein-coding gene in the species Homo sapiens

Mitochondrial ferritin is a ferroxidase enzyme that in humans is encoded by the FTMT gene.^[1]

It is classified as a metal-binding protein which is located within the mitochondria. After the protein is taken up by the mitochondria it can be processed into a mature protein and assemble functional ferritin shells.

Structure

Its structure was determined at 1.70 Å through the use of X-ray diffraction and contains 182 residues. It is 67% helical. The Ramachandran plot shows that the structure of mitochondrial ferritin is mainly alpha helical with a low prevalence of beta sheets.

References

↑ "A human mitochondrial ferritin encoded by an intronless gene". J. Biol. Chem. 276 (27): 24437–40. July 2001. doi:10.1074/jbc.C100141200. PMID 11323407.

"Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala.". J. Mol. Biol. 340 (2): 277–93. 2004. doi:10.1016/j.jmb.2004.04.036. PMID 15201052.
"The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin.". Biochim. Biophys. Acta 1782 (2): 90–8. 2008. doi:10.1016/j.bbadis.2007.11.006. PMID 18160053. https://hal.archives-ouvertes.fr/hal-00501557/file/PEER_stage2_10.1016%252Fj.bbadis.2007.11.006.pdf.
"Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo.". Biochem. J. 395 (3): 501–7. 2006. doi:10.1042/BJ20060063. PMID 16448386.
"Hemin-mediated regulation of an antioxidant-responsive element of the human ferritin H gene and role of Ref-1 during erythroid differentiation of K562 cells.". Mol. Cell. Biol. 26 (7): 2845–56. 2006. doi:10.1128/MCB.26.7.2845-2856.2006. PMID 16537925.
"Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation.". J. Biol. Chem. 283 (46): 31394–400. 2008. doi:10.1074/jbc.M806025200. PMID 18805796.
"Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia.". Blood 101 (5): 1996–2000. 2003. doi:10.1182/blood-2002-07-2006. PMID 12406866.
"Detection and functional analysis of an SNP in the promoter of the human ferritin H gene that modulates the gene expression.". Gene 377: 1–5. 2006. doi:10.1016/j.gene.2006.02.034. PMID 16797877.
"PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element.". J. Biol. Chem. 282 (31): 22335–43. 2007. doi:10.1074/jbc.M701477200. PMID 17565989.
"Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization.". Biochem. J. 411 (1): 107–13. 2008. doi:10.1042/BJ20071544. PMID 18076382.
"Mitochondrial ferritin: a new player in iron metabolism.". Blood Cells Mol. Dis. 29 (3): 376–83. 2002. doi:10.1006/bcmd.2002.0577. PMID 12547228.
"Ferritin: a novel mechanism for delivery of iron to the brain and other organs.". Am. J. Physiol., Cell Physiol. 293 (2): C641–9. 2007. doi:10.1152/ajpcell.00599.2006. PMID 17459943.
"Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia.". Hum. Mol. Genet. 18 (1): 1–11. 2009. doi:10.1093/hmg/ddn308. PMID 18815198.
"The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core.". Biochemistry 43 (14): 4332–7. 2004. doi:10.1021/bi0498813. PMID 15065877.
"Computational modeling of the dizinc-ferroxidase complex of human H ferritin: direct comparison of the density functional theory calculated and experimental structures.". J. Biol. Inorg. Chem. 14 (8): 1199–208. 2009. doi:10.1007/s00775-009-0563-z. PMID 19585161.
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
"Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
"Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress.". Free Radic. Biol. Med. 44 (9): 1762–71. 2008. doi:10.1016/j.freeradbiomed.2008.01.031. PMID 18325346.
"Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with Human H-chain ferritin.". J. Mol. Biol. 347 (3): 543–54. 2005. doi:10.1016/j.jmb.2005.01.007. PMID 15755449.
"p53-mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y.". Int. J. Biochem. Cell Biol. 40 (10): 2110–9. 2008. doi:10.1016/j.biocel.2008.02.010. PMID 18372207.
"Mitochondrial ferritin in the substantia nigra in restless legs syndrome.". J. Neuropathol. Exp. Neurol. 68 (11): 1193–9. 2009. doi:10.1097/NEN.0b013e3181bdc44f. PMID 19816198.

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Original source: https://en.wikipedia.org/wiki/Mitochondrial ferritin. Read more

[pmid11323407-1] "A human mitochondrial ferritin encoded by an intronless gene". J. Biol. Chem. 276 (27): 24437–40. July 2001. doi:10.1074/jbc.C100141200. PMID 11323407.

[1]

v t e Other oxidoreductases (EC 1.15-1.21)
1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3
1.16: Oxidizing metal ions	Ceruloplasmin
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
1.18: Acting on iron-sulfur proteins as donors	Nitrogenase
1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5
1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Mitochondrial ferritin

Topic: Biology

Structure

References

Further reading