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An archaeal homolog of proteasome assembly factor functions as a proteasome activator.

Kentaro Kumoi | Tadashi Satoh | Kazuyoshi Murata | Takeshi Hiromoto | Tsunehiro Mizushima | Yukiko Kamiya | Masanori Noda | Susumu Uchiyama | Hirokazu Yagi | Koichi Kato
PloS one | 2013

Assembly of the eukaryotic 20S proteasome is an ordered process involving several proteins operating as proteasome assembly factors including PAC1-PAC2 but archaeal 20S proteasome subunits can spontaneously assemble into an active cylindrical architecture. Recent bioinformatic analysis identified archaeal PAC1-PAC2 homologs PbaA and PbaB. However, it remains unclear whether such assembly factor-like proteins play an indispensable role in orchestration of proteasome subunits in archaea. We revealed that PbaB forms a homotetramer and exerts a dual function as an ATP-independent proteasome activator and a molecular chaperone through its tentacle-like C-terminal segments. Our findings provide insights into molecular evolution relationships between proteasome activators and assembly factors.

Pubmed ID: 23555947

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