RRC ID |
34471
|
著者 |
Sikdar A, Satoh T, Kawasaki M, Kato K.
|
タイトル |
Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA.
|
ジャーナル |
Biochem Biophys Res Commun
|
Abstract |
Formation of the eukaryotic proteasome is not a spontaneous process but a highly ordered process assisted by several assembly chaperones. In contrast, archaeal proteasome subunits can spontaneously assemble into an active form. Recent bioinformatic analysis identified the proteasome-assembly chaperone-like proteins, PbaA and PbaB, in archaea. Our previous study showed that the PbaB homotetramer functions as a proteasome activator through its tentacle-like C-terminal segments. However, a functional role of the other homolog PbaA has remained elusive. Here we determined the 2.25-Å resolution structure of PbaA, illustrating its disparate tertiary and quaternary structures compared with PbaB. PbaA forms a homopentamer in which the C-terminal segments, with a putative proteasome-activating motif, are packed against the core. These findings offer deeper insights into the molecular evolution relationships between the proteasome-assembly chaperones and the proteasome activators.
|
巻・号 |
453(3)
|
ページ |
493-7
|
公開日 |
2014-10-24
|
DOI |
10.1016/j.bbrc.2014.09.114
|
PII |
S0006-291X(14)01751-3
|
PMID |
25285636
|
MeSH |
Archaeal Proteins / chemistry*
Crystallography, X-Ray
Models, Molecular
Molecular Chaperones / chemistry*
Proteasome Endopeptidase Complex / chemistry*
Protein Conformation
|
IF |
2.985
|
引用数 |
2
|
WOS 分野
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
BIOPHYSICS
|
リソース情報 |
一般微生物 |
JCM 8422 |