| RRC ID |
34471
|
| Author |
Sikdar A, Satoh T, Kawasaki M, Kato K.
|
| Title |
Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA.
|
| Journal |
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.
|
| Volume |
453(3)
|
| Pages |
493-7
|
| Published |
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
|
| Times Cited |
2
|
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
BIOPHYSICS
|
| Resource |
| General Microbes |
JCM 8422 |
