Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in amphibia.

Dickey, Lynn F.; Sreedharan, Simmi P.; Theil, Elizabeth C.; Didsbury, John; Wang, Y H; Kaufman, Russel E.

doi:10.1016/s0021-9258(18)47653-3

Cited by 151 publications

(11 citation statements)

References 37 publications

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“…Site A and site B with either E, QxxD, or Q, QxxD formed DFP, but only with E, QxxD, was the K app and Hill coefficient equivalent to catalytically active wild-type ferritin. 23 Natural variations occur among maxiferritins at site B, D (RCOOH), S (RCH 2 OH), or A (RCH 3 ), 47,63 each with different di-iron oxidation kinetics. 23,64 The paths taken by ferrous ions to the catalytic sites and by the catalytic products (diferric oxy mineral precursors) to the mineralization cavity are not well understood in maxi-ferritins and even less understood in miniferritins.…”

Section: Function-iron Inmentioning

confidence: 99%

Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry

Liu¹,

Theil²

2005

Acc. Chem. Res.

463

369

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Ferritins are spherical, cage-like proteins with nanocavities formed by multiple polypeptide subunits (four-helix bundles) that manage iron/oxygen chemistry. Catalytic coupling yields diferric oxo/hydroxo complexes at ferroxidase sites in maxi-ferritin subunits (24 subunits, 480 kDa; plants, animals, microorganisms). Oxidation occurs at the cavity surface of mini-ferritins/Dps proteins (12 subunits, 240 kDa; bacteria). Oxidation products are concentrated as minerals in the nanocavity for iron-protein cofactor synthesis (maxi-ferritins) or DNA protection (mini-ferritins). The protein cage and nanocavity characterize all ferritins, although amino acid sequences diverge, especially in bacteria. Catalytic oxidation/di-iron coupling in the protein cage (maxi-ferritins, 480 kDa; plants, bacteria and animal cell-specific isoforms) or on the cavity surface (mini-ferritins/Dps proteins, 280 kDa; bacteria) initiates mineralization. Gated pores (eight or four), symmetrically arranged, control iron flow. The multiple ferritin functions combine pore, channel, and catalytic functions in compact protein structures required for life and disease response.

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Section: Function-iron Inmentioning

confidence: 99%

Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry

Liu¹,

Theil²

2005

Acc. Chem. Res.

463

369

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“…Ligands proposed as the site of initial ferroxidation, Glu58 and His61, related to rapid mineralization of H-subunit-type ferritin and based on Tb and Ca as models for Fe, were shown by site-directed mutagenesis to abolish rapid mineralization in H-subunit-type ferritin (Lawson, 1989(Lawson, , 1991Bauminger et al, 1992;Treffry et al, 1992). However, the same ligands are also found in a bullfrog ferritin (Dickey et al, 1987), recently shown to have the slow mineralization rates of L-subunit-type ferritin (Waldo et al, 1993). Clearly, these residues alone cannot explain the rapid rate of ferroxidation of Hversus L-subunit type ferritins.…”

mentioning

confidence: 98%

Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin

Waldo¹,

Theil²

1993

Biochemistry

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Rapid mineralization of ferritin, characteristic of protein with H-type subunits, coincides with formation of a specific Fe(III)-tyrosinate complex. The pseudo-first-order rate constant for Fe(II) oxidation by H-subunit-type ferritin has now been shown to be 700-900 times greater than any previously reported for ferritin; kox = 1000 s-1 for formation of the specific Fe(III)-tyrosinate complex (A550nm) or formation of less defined Fe(III)-oxo multinuclear complexes (A420nm). Formation of multinuclear Fe(III)-oxo complexes and O2 consumption were biphasic. In the first phase, up to 50 Fe atoms/ferritin molecule were rapidly oxidized, accompanied by formation of the Fe(III)-tyrosinate complex; saturation of the sites which formed the Fe(III)-tyrosinate complex also required 50 Fe/ferritin molecule. The sigmoidal shape of the curve obtained by plotting the initial rate of oxidation during the rapid phase of mineralization versus added [Fe(II)] suggested a more complex reaction pathway of ferroxidation than previously described. During the second phase of mineralization, Fe(III)-tyrosinate decreased, but multinuclear Fe(III)-oxo complexes and O2 consumption continued to increase at a slower rate. Recovery of the rapid oxidation pathway paralleled recovery of the site for Fe(III)-tyrosinate formation; full regeneration of the Fe(III)-tyrosinate sites was gradual over a period of 12 h, as if the movement of Fe(III) along the biomineralization pathway in the protein was slow and was accompanied by conformational changes which affected the Fe(III)-tyrosinate site.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…In most species, there are two forms of the protein subunits with molecular weights of about 21000 for the heavy (H) chain and 19000 for the light (L) subunit (Theil, 1987). In bullfrogs, an additional subunit (M) of intermediate molecular weight has been identified (Dickey et al, 1987). Ferritin is very abundant in the liver.…”

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confidence: 99%

“…Ferritin is very abundant in the liver. The L subunit predominates in mammalian liver (Arosio et al, 1978), but Dickey et al (1987) showed that M-subunit mRNA predominates in Rana liver and suggested that in mammals a comparable form may exist that has been mistakenly designated L. Complementary DNA clones for both the H and L subunits have been characterized from several species (Brown et al, 1983; Leibold et al, 1984; Dorner et al, 1985;Boyd et al, 1985;Dickey et al, 1987). The two subunits are synthesized from mRNAs ©1991 American Chemical Society about 1000 nucleotides in length and are encoded by evolutionarily related gene families (Jain et al, 1985;Santoro et al" 1986;Stevens et al, 1987; Leibold & Munro, 1987).…”

mentioning

confidence: 99%

“…The two subunits are synthesized from mRNAs ©1991 American Chemical Society about 1000 nucleotides in length and are encoded by evolutionarily related gene families (Jain et al, 1985;Santoro et al" 1986;Stevens et al, 1987; Leibold & Munro, 1987). Changes in ferritin mRNA levels occur in many cell types during development (Dickey et al, 1987) and differentiation (Chou et al, 1986), and in response to a variety of agents (Torti et al, 1988;Cox et al, 1988). In addition to regulation at the mRNA level, translational utilization is a major means of control of ferritin production.…”

mentioning

confidence: 99%

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Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment

Holland¹,

Wall²,

Bhattacharya³

1991

Biochemistry

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In vitro translation of liver mRNA from estrogen-treated Xenopus frogs yields two abundant polypeptides in the range of 20 kDa. DNA clones for one of these translation products were isolated and shown to be complementary to mRNA for the heavy subunit of ferritin. The predicted Xenopus amino acid sequence shares about 86% identity with the ferritin heavy chain from bullfrogs and about 70% identity with the comparable mammalian and avian proteins. Clone identity was confirmed by hybridization selection followed by in vitro translation into translation products of 19.5-20 kDa. The nearly full-length cDNA clone, termed XlferH1, comprises 868 nucleotides plus 22 adenosines of the poly(A) tail, including 134 nucleotides of the 5'-untranslated region, a 528-base coding region for 176 amino acids, and a 206-nucleotide 3'-untranslated region. The clone lacks 22 nucleotides from the 5' end of the mRNA. The level of ferritin mRNA in the liver of estrogen-treated frogs was determined over time. The amount of this mRNA relative to total RNA decreased about 3-fold 14 days after estradiol-17 beta was administered. However, the hormone also elevated total RNA in the liver about 24-fold. Hence, the total ferritin mRNA content of the liver increased to about 8 times its initial amount. This pattern of gene expression was very similar to that for serum retinol binding protein. The estrogen induction of these two mRNAs appeared to parallel the overall stimulation of hepatic RNA synthesis.(ABSTRACT TRUNCATED AT 250 WORDS)

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Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in amphibia.

Cited by 151 publications

References 37 publications

Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry

Ferritins: Dynamic Management of Biological Iron and Oxygen Chemistry

Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin

Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment

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