PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor

Autor: S. J. Gunn, Jacob Hooper, Thomas Lanyon-Hogg, Alison Baker, Stuart L. Warriner
Jazyk: angličtina
Předmět:
Peroxisome-Targeting Signal 1 Receptor
Arabidopsis thaliana
Biophysics
Arabidopsis
Receptors
Cytoplasmic and Nuclear
Plasma protein binding
macromolecular substances
PMP
peroxisomal membrane protein
Peroxisome
PEX14
Biochemistry
environment and public health
Article
law.invention
Structural Biology
law
Genetics
Receptor
Molecular Biology
Peroxisomal targeting signal
FI
fluorescence intensity
Peroxisomal Targeting Signal 2 Receptor
biology
Thiolase
Arabidopsis Proteins
FA
fluorescence anisotropy
Membrane Proteins
HRP
horseradish peroxidase
Cell Biology
PEX7
biology.organism_classification
PEX5
Cell biology
Transport protein
PTS
peroxisomal targeting signal
Repressor Proteins
Kinetics
Protein Transport
Membrane protein
PEX
peroxisome biogenesis
Recombinant DNA
PTS2
PTS1
Protein Binding
Cargo unloading
Zdroj: Febs Letters
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2014.05.038
Popis: Highlights • The interaction between Arabidopsis PEX5 and PEX14N is independent of cargo binding. • The affinity of a PTS1 peptide for PEX5 is unaffected by PEX14N binding. • Arabidopsis PEX5 complexes PTS1 and PTS2 cargoes. • PEX5 and 7 co-isolate with PEX14N, but the PTS2 cargo thiolase does not. • PEX14N does not unload canonical PTS1 cargo peptide in vitro but may play a role in PTS2 release.
PEX5 acts as a cycling receptor for import of PTS1 proteins into peroxisomes and as a co-receptor for PEX7, the PTS2 receptor, but the mechanism of cargo unloading has remained obscure. Using recombinant protein domains we show PEX5 binding to the PEX14N-terminal domain (PEX14N) has no effect on the affinity of PEX5 for a PTS1 containing peptide. PEX5 can form a complex containing both recombinant PTS1 cargo and endogenous PEX7-thiolase simultaneously but isolation of the complex via the PEX14 construct resulted in an absence of thiolase, suggesting a possible role for PEX14 in the unloading of PTS2 cargos.
Structured summary of protein interactions pMDH1physically interacts with PEX5 by pull down (View interaction) PEX5Cbinds to PEX14N by filter binding (View interaction) PEX14Nbinds to PEX5C by pull down (View interaction) PEX14Nphysically interacts with PEX7 by pull down (View interaction) PEX5physically interacts with PEX7 by pull down (View interaction) DCI1physically interacts with PEX5 by pull down (View interaction) PEX5physically interacts with thiolase PTS2-cargo by pull down (View interaction) pMDH1physically interacts with PEX7 by pull down (View interaction) DCI1physically interacts with thiolase PTS2-cargo by pull down (View interaction) DCI1physically interacts with PEX7 by pull down (View interaction) PEX14Nphysically interacts with PEX5 by pull down (View interaction)
Databáze: OpenAIRE
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