Structural and bioinformatics analyses identify deoxydinucleotide-specific nucleases and their association with genomic islands in gram-positive bacteria.

Dinucleases of the DEDD superfamily, such as oligoribonuclease, Rexo2 and nanoRNase C, catalyze the essential final step of RNA degradation, the conversion of di- to mononucleotides. The active sites of these enzymes are optimized for substrates that are two nucleotides long, and do not discriminate between RNA and DNA. Here, we identified a novel DEDD subfamily, members of which function as dedicated deoxydinucleases (diDNases) that specifically hydrolyze single-stranded DNA dinucleotides in a sequence-independent manner.

Diribonuclease activity eliminates toxic diribonucleotide accumulation.

RNA degradation is a central process required for transcriptional regulation. Eventually, this process degrades diribonucleotides into mononucleotides by specific diribonucleases. In Escherichia coli, oligoribonuclease (Orn) serves this function and is unique as the only essential exoribonuclease.

Neolithic Yersinia pestis infections in humans and a dog.

Yersinia pestis has been infecting humans since the Late Neolithic (LN). Whether those early infections were isolated zoonoses or initiators of a pandemic remains unclear. We report Y.

Reconstitution of a biofilm adhesin system from a sulfate-reducing bacterium in .

Biofilms of sulfate-reducing bacterium (SRB) like Hildenborough (DvH) can facilitate metal corrosion in various industrial and environmental settings leading to substantial economic losses. Although the mechanisms of biofilm formation by DvH are not yet well understood, recent studies indicate the large adhesin, DvhA, is a key determinant of biofilm formation. The gene neighborhood resembles the biofilm-regulating Lap system of but is curiously missing the c-di-GMP-binding regulator LapD.

Reconstitution of a Biofilm Adhesin System from a Sulfate-Reducing Bacterium in .

Biofilms of the sulfate reducing bacterium (SRB) Hildenborough (DvH) can facilitate metal corrosion in various industrial and environmental settings leading to substantial economic losses; however, the mechanisms of biofilm formation by DvH are not yet well-understood. Evidence suggests that a large adhesin, DvhA, may be contributing to biofilm formation in DvH. The gene and its neighbors encode proteins that resemble the Lap system, which regulates biofilm formation by , including a LapG-like protease DvhG and effector protein DvhD, which has key differences from the previously described LapD.