Bacterial proteasome and PafA, the pup ligase, interact to form a modular protein tagging and degradation machine.
Proteasome-containing bacteria possess a tagging system that directs proteins to proteasomal degradation by conjugating them to a prokaryotic ubiquitin-like protein (Pup). A single ligating enzyme, PafA, is responsible for Pup conjugation to lysine side chains of protein substrates. As Pup is recognized by the regulatory subunit of the proteasome, Pup functions as a degradation tag. Pup presents overlapping regions for binding of the proteasome and PafA. It was, therefore, unclear whether Pup binding by the proteasome regulatory subunit, Mpa, and by PafA are mutually exclusive events. The work presented here provides evidence for the simultaneous interaction of Pup with both Mpa and PafA. Surprisingly, we found that PafA and Mpa can form a complex both in vitro and in vivo. Our results thus suggest that PafA and the proteasome can function as a modular machine for the tagging and degradation of cytoplasmic proteins.
Department of Life Sciences and ‡The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev , Beer-Sheva 84105, Israel.
Nadav
N
Forer
Maayan
M
Korman
Yifat
Y
Elharar
Marina
M
Vishkautzan
Eyal
E
Gur
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D020102:Mycobacterium smegmatis / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry / Q000378:metabolism*; D059748:Proteolysis; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex