Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ribosomal frameshifting is a translational mechanism used as an essential step in the replication cycle of retroviruses. Programmed frameshifting in retroviral translation involves two sequence elements: A heptanucleotide slippery sequence which induces a low basal level of frameshifting and a downstream RNA structure as an enhancer of the process. The precise mechanism of function of these downstream elements is still unclear, but their effect does not solely depend on their stability. Likewise, the possibility that frameshifting could be controlled by specific proteins that bind to these elements and enable or modulate their effects has yet not been substantiated. The RNA hairpin of the HIV-1 gag-pol frameshift cassette was replaced by the iron-responsive element (IRE) from ferritin mRNA, a stem-loop structure that binds iron regulatory proteins (IRPs) in dependence of the iron status of the cell. When a lacZ/luciferase reporter construct was expressed in transfected BHK-21 cells, the IRE or a point-mutated version that is unable to bind IRPs were found to functionally substitute for the HIV-1 hairpin. When cells were treated with the iron chelator desferrioxamine to stimulate IRP binding to the wild-type IRE, frameshift activity was specifically and strongly augmented by protein binding Our data establish that frameshifting can be regulated in a reversible fashion by mRNA-binding proteins.
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PMID:Regulated ribosomal frameshifting by an RNA-protein interaction. 863 12

Polydisulfides of urea (PDSU), thiourea (PDSTU), biuret (PDSB), and gallic acid (PDSG) and their monomer analogues (urea, biuret, and gallic acid) inhibited (in a competitive manner) tetramethylbenzidine (TMB) peroxidation catalyzed by ferritin in 0.1 M acetate buffer, pH 4.2, containing 10% dimethylformamide. Their efficiency characterized in terms of inhibition constants, Ki, increased in the following order PDSU < PDSB approximately PDSTU << PDSG. This order is determined by the reactivity of monomers with respect to HO* radicals which are the main oxidizing agents in the system ferritin--H2O2. Polydisulfide antioxidants exhibit the intramolecular synergism of the inhibiting action (non-additivity of antiradical activity relative to their monomers) that was quantitatively characterized by alpha = (Ki)pol/(Ki)mon x n, where n is the number of monomers in the polymeric inhibitors. The alpha values increased from 1.5 up to 5.18 in the following order: PDSG < PDSU < PDSB. Significantly higher inhibiting efficiency of polydisulfide antioxidants as compared to monomer forms and synergism of the inhibitory action offer promising opportunities of their use as quenchers of free radical processes in biochemical systems.
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PMID:Intramolecular synergism of the inhibiting action of polydisulfide antioxidants in the system ferritin--H2O2--tetramethylbenzidine. 1056 69

The exosome-independent exoribonuclease DIS3L2 is mutated in Perlman syndrome. Here, we used extensive global transcriptomic and targeted biochemical analyses to identify novel DIS3L2 substrates in human cells. We show that DIS3L2 regulates pol II transcripts, comprising selected canonical and histone-coding mRNAs, and a novel FTL_short RNA from the ferritin mRNA 5' UTR. Importantly, DIS3L2 contributes to surveillance of maturing snRNAs during their cytoplasmic processing. Among pol III transcripts, DIS3L2 particularly targets vault and Y RNAs and an Alu-like element BC200 RNA, but not Alu repeats, which are removed by exosome-associated DIS3. Using 3' RACE-Seq, we demonstrate that all novel DIS3L2 substrates are uridylated in vivo by TUT4/TUT7 poly(U) polymerases. Uridylation-dependent DIS3L2-mediated decay can be recapitulated in vitro, thus reinforcing the tight cooperation between DIS3L2 and TUTases. Together these results indicate that catalytically inactive DIS3L2, characteristic of Perlman syndrome, can lead to deregulation of its target RNAs to disturb transcriptome homeostasis.
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PMID:Perlman syndrome nuclease DIS3L2 controls cytoplasmic non-coding RNAs and provides surveillance pathway for maturing snRNAs. 2743 25