Overcoming lysogenization defect (OLD) proteins are a conserved family of ATP‐powered
nucleases that function in anti‐phage defense. Recent bioinformatic, genetic, and …

Bacteriophages constitute a ubiquitous threat to bacteria, and bacteria have evolved
numerous anti-phage defense systems to protect themselves. These systems include well …

Overcoming lysogenization defect (OLD) proteins constitute a family of uncharacterized
nucleases present in bacteria, archaea, and some viruses. These enzymes contain an N …

OLD family nucleases contain an N-terminal ATPase domain and a C-terminal Toprim
domain. Homologs segregate into two classes based on primary sequence length and the …

Coupling distinct enzymatic effectors emerges as an efficient strategy for defense against
phage infection in bacterial immune responses, such as the widely studied nuclease and …

Nucleases cleave the phosphodiester bonds of nucleic acids and may be endo or exo,
DNase or RNase, topoisomerases, recombinases, ribozymes, or RNA splicing enzymes. In …

Pseudomonas phages are increasingly important biomedicines for phage therapy, but little
is known about how these viruses package DNA. This paper explores the terminase …

His-Me finger (also called HNH or ββα-me) nucleases, are a large superfamily of nucleases
that share limited sequence homology, but all members carry a highly similar catalytic motif …

Genome sequencing projects have focused attention on the problem of discovering the
functions of protein domains that are widely distributed throughout living species but which …

Nucleases are a super family of enzymes that hydrolyze phosphodiester bonds present in
genomes. They widely vary in substrates, causing differentiation in cleavage patterns and …