scholarly journals A novel dynein-type AAA+ protein with peroxisomal targeting signal type 2

2020 ◽  
Vol 167 (5) ◽  
pp. 429-432
Author(s):  
Tsuneo Imanaka ◽  
Kosuke Kawaguchi
Keyword(s):  
Mammalian Cells ◽  
Ring Structure ◽  
Family Protein ◽  
Peroxisomal Targeting ◽  
Signal Type ◽  
Targeting Signal ◽  
Aaa Protein ◽  
Peroxisomal Targeting Signal

Abstract 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.

scholarly journals Recognition of Peroxisomal Targeting Signal Type 1 by the Import Receptor Pex5p

2001 ◽  
Vol 276 (18) ◽  
pp. 15034-15041 ◽  
Author(s):  
André T. J. Klein ◽  
Phil Barnett ◽  
Gina Bottger ◽  
Daphne Konings ◽  
Henk F. Tabak ◽  
...  
Keyword(s):  
Peroxisomal Targeting ◽  
Signal Type ◽  
Targeting Signal ◽  
Peroxisomal Targeting Signal ◽  
Import Receptor

scholarly journals Distinct Ubiquitination Cascades Act on the Peroxisomal Targeting Signal Type 2 Co-receptor Pex18p

Traffic ◽  
2013 ◽  
Vol 14 (12) ◽  
pp. 1290-1301 ◽  
Author(s):  
Fouzi El Magraoui ◽  
Rebecca Brinkmeier ◽  
Andreas Schrötter ◽  
Wolfgang Girzalsky ◽  
Thorsten Müller ◽  
...  
Keyword(s):  
Peroxisomal Targeting ◽  
Signal Type ◽  
Targeting Signal ◽  
Peroxisomal Targeting Signal

scholarly journals Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor.

1996 ◽  
Vol 135 (1) ◽  
pp. 85-95 ◽  
Author(s):  
S J Gould ◽  
J E Kalish ◽  
J C Morrell ◽  
J Bjorkman ◽  
A J Urquhart ◽  
...  
Keyword(s):  
Steady State ◽  
Matrix Proteins ◽  
Cytoplasmic Protein ◽  
Peroxisomal Membrane ◽  
Peroxisomal Targeting ◽  
Targeting Signal ◽  
Peroxisome Membrane ◽  
Peroxisomal Targeting Signal

Import of newly synthesized PTS1 proteins into the peroxisome requires the PTS1 receptor (Pex5p), a predominantly cytoplasmic protein that cycles between the cytoplasm and peroxisome. We have identified Pex13p, a novel integral peroxisomal membrane from both yeast and humans that binds the PTS1 receptor via a cytoplasmically oriented SH3 domain. Although only a small amount of Pex5p is bound to peroxisomes at steady state (< 5%), loss of Pex13p further reduces the amount of peroxisome-associated Pex5p by approximately 40-fold. Furthermore, loss of Pex13p eliminates import of peroxisomal matrix proteins that contain either the type-1 or type-2 peroxisomal targeting signal but does not affect targeting and insertion of integral peroxisomal membrane proteins. We conclude that Pex13p functions as a docking factor for the predominantly cytoplasmic PTS1 receptor.

scholarly journals A PEX7-Centered Perspective on the Peroxisomal Targeting Signal Type 2-Mediated Protein Import Pathway

2014 ◽  
Vol 34 (15) ◽  
pp. 2917-2928 ◽  
Author(s):  
T. A. Rodrigues ◽  
I. S. Alencastre ◽  
T. Francisco ◽  
P. Brites ◽  
M. Fransen ◽  
...  
Keyword(s):  
Protein Import ◽  
Peroxisomal Targeting ◽  
Signal Type ◽  
Targeting Signal ◽  
Peroxisomal Targeting Signal

scholarly journals Peroxisomal lactate dehydrogenase is generated by translational readthrough in mammals

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Fabian Schueren ◽  
Thomas Lingner ◽  
Rosemol George ◽  
Julia Hofhuis ◽  
Corinna Dickel ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
In Silico ◽  
Stop Codon ◽  
The Other ◽  
Translational Readthrough ◽  
Peroxisomal Targeting ◽  
Signal Type ◽  
Targeting Signal ◽  
Peroxisomal Targeting Signal

Translational readthrough gives rise to low abundance proteins with C-terminal extensions beyond the stop codon. To identify functional translational readthrough, we estimated the readthrough propensity (RTP) of all stop codon contexts of the human genome by a new regression model in silico, identified a nucleotide consensus motif for high RTP by using this model, and analyzed all readthrough extensions in silico with a new predictor for peroxisomal targeting signal type 1 (PTS1). Lactate dehydrogenase B (LDHB) showed the highest combined RTP and PTS1 probability. Experimentally we show that at least 1.6% of the total cellular LDHB is targeted to the peroxisome by a conserved hidden PTS1. The readthrough-extended lactate dehydrogenase subunit LDHBx can also co-import LDHA, the other LDH subunit, into peroxisomes. Peroxisomal LDH is conserved in mammals and likely contributes to redox equivalent regeneration in peroxisomes.

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