Autor: |
Kentaro Kumoi, Tadashi Satoh, Kazuyoshi Murata, Takeshi Hiromoto, Tsunehiro Mizushima, Yukiko Kamiya, Masanori Noda, Susumu Uchiyama, Hirokazu Yagi, Koichi Kato |
Jazyk: |
angličtina |
Rok vydání: |
2013 |
Předmět: |
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Zdroj: |
PLoS ONE, Vol 8, Iss 3, p e60294 (2013) |
Druh dokumentu: |
article |
ISSN: |
1932-6203 |
DOI: |
10.1371/journal.pone.0060294 |
Popis: |
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. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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