| RRC ID |
29299
|
| Author |
Kumoi K, Satoh T, Murata K, Hiromoto T, Mizushima T, Kamiya Y, Noda M, Uchiyama S, Yagi H, Kato K.
|
| Title |
An archaeal homolog of proteasome assembly factor functions as a proteasome activator.
|
| Journal |
PLoS One
|
| Abstract |
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.
|
| Volume |
8(3)
|
| Pages |
e60294
|
| Published |
2013-1-1
|
| DOI |
10.1371/journal.pone.0060294
|
| PII |
PONE-D-12-23454
|
| PMID |
23555947
|
| PMC |
PMC3605417
|
| MeSH |
Archaea / metabolism*
Archaeal Proteins / metabolism*
Evolution, Molecular
Proteasome Endopeptidase Complex / metabolism*
Protein Binding
|
| IF |
2.74
|
| Times Cited |
13
|
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| DNA material |
Genomic DNA of Pyrococcus furiosus JCM 8422T (JGD07704) |
| General Microbes |
JCM 8422 |
