PMID- 18718908
OWN - NLM
STAT- MEDLINE
DCOM- 20090107
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 283
IP  - 46
DP  - 2008 Nov 14
TI  - Leishmania donovani peroxin 14 undergoes a marked conformational change following 
      association with peroxin 5.
PG  - 31488-99
LID - 10.1074/jbc.M803529200 [doi]
AB  - The import of PTS1 proteins into the glycosome or peroxisome requires binding of 
      a PTS1-laden PEX5 receptor to the membrane-associated protein PEX14 to facilitate 
      translocation of PTS1 proteins into the lumen of these organelles. Quaternary 
      structure analysis of protozoan parasite Leishmania donovani PEX14 (LdPEX14) 
      revealed that this protein forms a homomeric complex with a size > 670 kDa. 
      Moreover, deletion mapping indicated that disruption of LdPEX14 oligomerization 
      correlated with the elimination of the hydrophobic region and coiled-coil motif 
      present in LdPEX14. Analysis of the LdPEX5-LdPEX14 interaction by isothermal 
      titration calorimetry revealed a molar binding stoichiometry of 1:4 (LdPEX5: 
      LdPEX14) and an in-solution dissociation constant (K(d)) of approximately 74 nm. 
      Calorimetry, circular dichroism, intrinsic fluorescence, and analytical 
      ultracentrifugation experiments showed that binding of LdPEX5 resulted in a 
      dramatic conformational change in the LdPEX14 oligomeric complex that involved 
      the reorganization of the hydrophobic segment in LdPEX14. Finally, limited 
      tryptic proteolysis assays established that in the presence of LdPEX5, LdPEX14 
      became more susceptible to proteolytic degradation consistent with this protein 
      interaction triggering a significant conformational change in the recombinant and 
      native LdPEX14 structures. These structural changes provide essential clues to 
      how LdPEX14 functions in the translocation of folded proteins across the 
      glycosomal membrane.
FAU - Cyr, Normand
AU  - Cyr N
AD  - Institute of Parasitology, Macdonald Campus of McGill University, 
      Ste-Anne-de-Bellevue, Quebec H9X 3V9.
FAU - Madrid, Kleber P
AU  - Madrid KP
FAU - Strasser, Rona
AU  - Strasser R
FAU - Aurousseau, Mark
AU  - Aurousseau M
FAU - Finn, Ron
AU  - Finn R
FAU - Ausio, Juan
AU  - Ausio J
FAU - Jardim, Armando
AU  - Jardim A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080821
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - EC 3.4.- (Peptide Hydrolases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Calorimetry
MH  - Circular Dichroism
MH  - Leishmania donovani/*chemistry/genetics/*metabolism
MH  - Membrane Proteins/*chemistry/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Peptide Hydrolases/metabolism
MH  - Protein Binding
MH  - Protein Structure, Quaternary
MH  - Receptors, Cytoplasmic and Nuclear/*chemistry/genetics/*metabolism
MH  - Thermodynamics
EDAT- 2008/08/23 09:00
MHDA- 2009/01/08 09:00
CRDT- 2008/08/23 09:00
PHST- 2008/08/23 09:00 [pubmed]
PHST- 2009/01/08 09:00 [medline]
PHST- 2008/08/23 09:00 [entrez]
AID - S0021-9258(20)56890-7 [pii]
AID - 10.1074/jbc.M803529200 [doi]
PST - ppublish
SO  - J Biol Chem. 2008 Nov 14;283(46):31488-99. doi: 10.1074/jbc.M803529200. Epub 2008 
      Aug 21.