Uracil in DNA is usually considered to be an error, but it may be used for
signaling in Drosophiladevelopment via recognition by a novel uracil-DNA-degrading factor (UDE) [(Bekesi Aet al. (2007) Biochem Biophys
Res Commun355, 643–648]. The UDE protein has no detectable similarity
to any other uracil-DNA-binding factors, and has no structurally or func-tionally described homologs.
DPP IV has been attributed a large array of functions, some of which are mediated by
its exopeptidase activity. Although it only removes two amino acid residues at the N-terminus
of the peptide, this cleavage can inactivate or modify the activity of regulatory peptides, peptide
hormones, chemokines and neuropeptides. Several excellent DPP IV substrates with high
specificity constants were identified by the in vitro kinetic study of the truncation of bioactive
peptides by DPP IV. In vivo studies e.g.
Oviparously developing embryos of the brine shrimp, Artemia franciscana, synthesize abundant quantities of a small heat shock/a-crystallin protein, termed p26. Wild-type p26 functions as a molecular chaperone in vitro and is thought to help encysted Artemia embryos survive severe physiological stress encountered during diapause and anoxia. Full-length and truncated p26 cDNA derivatives were generated by PCR ampliﬁcation of p26-3-6-3, then cloned in either pET21(+) or pRSETC and expressed in Escherichia coli BL21(DE3)....