Catalytic properties and biological function of a PIWI-RE nuclease from Pseudomonas stutzeri.

ABSTRACT:

Background

Prokaryotic Argonaute (pAgo) proteins are well-known oligonucleotide-directed endonucleases, which contain a conserved PIWI domain required for endonuclease activity. Distantly related to pAgos, PIWI-RE family, which is defined as PIWI with conserved R and E residues, has been suggested to exhibit divergent activities. The distinctive biochemical properties and physiological functions of PIWI-RE family members need to be elucidated to explore their applications in gene editing.

Results

Here, we describe the catalytic performance and cellular functions of a PIWI-RE family protein from Pseudomonas stutzeri (PsPIWI-RE). Structural modelling suggests that the protein possesses a PIWI structure similar to that of pAgo, but with different PAZ-like and N-terminal domains

SUBMITTER: Huang F 

PROVIDER: S-EPMC10991935 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature