Structural highlights
Publication Abstract from PubMed
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.
An archaeal homolog of proteasome assembly factor functions as a proteasome activator.,Kumoi K, Satoh T, Murata K, Hiromoto T, Mizushima T, Kamiya Y, Noda M, Uchiyama S, Yagi H, Kato K PLoS One. 2013;8(3):e60294. doi: 10.1371/journal.pone.0060294. Epub 2013 Mar 21. PMID:23555947[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumoi K, Satoh T, Murata K, Hiromoto T, Mizushima T, Kamiya Y, Noda M, Uchiyama S, Yagi H, Kato K. An archaeal homolog of proteasome assembly factor functions as a proteasome activator. PLoS One. 2013;8(3):e60294. doi: 10.1371/journal.pone.0060294. Epub 2013 Mar 21. PMID:23555947 doi:10.1371/journal.pone.0060294
