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Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
The different catalytic properties and the different subnuclear localization patterns shown by the human homologues indicate that hABH2 and hABh3 have distinct roles in the cellular response to alkylation damage, which is important for establishing RNA repair as a potentially important defence mechanism in living cells.
AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
It is shown that AlkB from Escherichia coli is indeed a 2-oxoglutarate-dependent and iron-dependent DNA repair enzyme that releases replication blocks in alkylated DNA by a mechanism involving oxidative demethylation of 1-methyladenine residues.
Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol.
The finding that glycosylated A chain was present in the cytosol indicates that translocation takes place after transport of the toxin to the ER.
Mammalian ALKBH8 Possesses tRNA Methyltransferase Activity Required for the Biogenesis of Multiple Wobble Uridine Modifications Implicated in Translational Decoding
It is shown here that ALKBh8 is a tRNA methyltransferase required for the final step in the biogenesis of mcm5U, and that the interaction of ALKBH8 with a small accessory protein, TRM112, is required to form a functional tRNAmethyltransferase.
AlkB restores the biological function of mRNA and tRNA inactivated by chemical methylation.
It is demonstrated that AlkB proteins can mediate functional recovery of RNA exposed to methylation damage, supporting the notion that RNA repair is important.
Repair deficient mice reveal mABH2 as the primary oxidative demethylase for repairing 1meA and 3meC lesions in DNA
It is found that in vitro repair of 1meA and 3meC in double‐stranded DNA by nuclear extracts depended primarily, if not solely, on mABH2, and the data suggest that m ABH2 andmABH3 have different roles in the defense against alkylating agents.
Penetration of protein toxins into cells.
Some AB-toxins depend on retrograde transport through the secretory pathway to the ER before translocation, and recent findings suggest that these toxins take advantage of the ER translocation machinery normally used for transport of cellular proteins.
Repair of 3-methylthymine and 1-methylguanine lesions by bacterial and human AlkB proteins.
  • P. Falnes
  • Biology, Medicine
    Nucleic acids research
  • 2004
The data show that 3-meT and 1-meG are repaired by AlkB, but indicate that the recognition of these substrates is different from that in the case of 1-MeA and 3-MeC.
Substrate specificities of bacterial and human AlkB proteins.
The results generally confirm the notion that while AlkB and hABH3 tend to prefer single-stranded nucleic acids, h ABH2 is more active on double-stranding substrates, and may contribute to identifying the main substrates of bacterial and human AlkB proteins in vivo.
Characterization of membrane translocation by anthrax protective antigen.
An assay for translocation in which radiolabeled ligands are bound to proteolytically activated PA at the surface of CHO or L6 cells, and translocation across the plasma membrane is induced by lowering the pH demonstrates that the acid-induced translocation by anthrax toxin closely resembles that of diphtheria toxin, despite the fact that these two toxins are unrelated and form pores by different mechanisms.