A novel dynein-type AAA+ protein with peroxisomal targeting signal type 2.
ATPase
Pex7p
dynein-type AAA+
mitochondria
peroxisomal targeting signal
peroxisome
Journal
Journal of biochemistry
ISSN: 1756-2651
Titre abrégé: J Biochem
Pays: England
ID NLM: 0376600
Informations de publication
Date de publication:
01 May 2020
01 May 2020
Historique:
received:
08
01
2020
accepted:
28
01
2020
pubmed:
7
2
2020
medline:
7
2
2021
entrez:
7
2
2020
Statut:
ppublish
Résumé
Peroxisomal matrix proteins are imported into peroxisomes in a process mediated by peroxisomal targeting signal (PTS) type 1 and 2. The PTS2 proteins are imported into peroxisomes after binding with Pex7p. Niwa et al. (A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel dynein-type AAA+ protein. J Biochem 2018;164:437-447) identified a novel Pex7p-binding protein in CHO cells and characterized the subcellular distribution and molecular properties of the human homologue, 'P7BP2'. Interestingly, P7BP2 possesses PTS2 at the NH2 terminal and six putative AAA+ domains. Another group has suggested that the protein also possesses mitochondrial targeting signal at the NH2 terminal. In fact, the P7BP2 expressed in mammalian cells is targeted to both peroxisomes and mitochondria. The purified protein from Sf9 cells is a monomer and has a disc-like ring structure, suggesting that P7BP2 is a novel dynein-type AAA+ family protein. The protein expressed in insect cells exhibits ATPase activity. P7BP2 localizes to peroxisomes and mitochondria, and has a common function related to dynein-type ATPases in both organelles.
Identifiants
pubmed: 32027355
pii: 5728638
doi: 10.1093/jb/mvaa018
doi:
Substances chimiques
Peroxisomal Targeting Signals
0
Adenosine Triphosphatases
EC 3.6.1.-
VWA8 protein, human
EC 3.6.1.3
Dyneins
EC 3.6.4.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
429-432Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.