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