Genetic and biochemical analyses reveal that the bacterial nucleases PNPase and RNase R work in concert with a type III-A CRISPR-Cas immune system to process small CRISPR RNAs and ensure robust immunity against foreign nucleic acid invaders.

Degradosome-associated nucleases PNPase and RNase J2 are required for type III CRISPR immunity against diverse nucleic acid invaders originating from plasmid and phage.

Cooperation between evolutionarily disparate CRISPR-Cas modules allows bacteria to counter mutational escape by viruses.

A widespread ribonuclease is a CRISPR-associated ring nuclease with a highly unusual cooperative mechanism involving tetramerisation of the enzyme.

Three-dimensional structure of CRISPR Cas7-11 shed light on protein evolution and guide development of biotechnology for RNA manipulations in cells.

Generation of the anti-viral second messenger cyclic oligoadenylate by type III CRISPR systems is tightly controlled in response to viral RNA load and sequence.

The dynamic interplay between type III CRISPR enzymes governs cyclic nucleotide levels and infection outcomes in virus-host conflict.

Bacterial Type IV restriction-modification systems display remarkable, previously unnoticed diversity of complex gene and domain architectures, and are predicted to couple antiphage immunity with the abortive infection form of defense.

Expression pattern analysis of neurotransmitter synthesis, secretion, and reuptake machinery reveals animal-wide usage of neurotransmitters in both sexes of Caenorhabditis elegans.