Bacterial proteasome and PafA, the Pup ligase, interact to form a modular protein tagging and degradation machine

Nadav Forer, Maayan Korman, Yifat Elharar, Marina Vishkautzan, Eyal Gur

פרסום מחקרי: פרסום בכתב עתמאמרביקורת עמיתים

תקציר

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.

שפה מקוריתאנגלית אמריקאית
עמודים (מ-עד)9029-9035
מספר עמודים7
כתב עתBiochemistry
כרך52
מספר גיליון50
מזהי עצם דיגיטלי (DOIs)
סטטוס פרסוםפורסם - 17 דצמ׳ 2013

ASJC Scopus subject areas

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