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Title: ZmPUMP encodes a fully functional monocot plant uncoupling mitochondrial protein whose affinity to fatty acid is increased with the introduction of a His pair at the second matrix loop

Abstract

Uncoupling proteins (UCPs) are specialized mitochondrial transporter proteins that uncouple respiration from ATP synthesis. In this study, cDNA encoding maize uncoupling protein (ZmPUMP) was expressed in Escherichia coli and recombinant ZmPUMP reconstituted in liposomes. ZmPUMP activity was associated with a linoleic acid (LA)-mediated H{sup +} efflux with K {sub m} of 56.36 {+-} 0.27 {mu}M and V {sub max} of 66.9 {mu}mol H{sup +} min{sup -1} (mg prot){sup -1}. LA-mediated H{sup +} fluxes were sensitive to ATP inhibition with K {sub i} of 2.61 {+-} 0.36 mM (at pH 7.2), a value similar to those for dicot UCPs. ZmPUMP was also used to investigate the importance of a histidine pair present in the second matrix loop of mammalian UCP1 and absent in plant UCPs. ZmPUMP with introduced His pair (Lys155His and Ala157His) displayed a 1.55-fold increase in LA-affinity while its activity remained unchanged. Our data indicate conserved properties of plant UCPs and suggest an enhancing but not essential role of the histidine pair in proton transport mechanism.

Authors:
 [1];  [2];  [1];  [1]
  1. Instituto de Biociencias, Departamento de Genetica, UNESP, Botucatu, SP (Brazil)
  2. Laboratorio de Bioenergetica, Faculdade de Ciencias Medicas (NMCE), UNICAMP, Campinas, SP (Brazil)
Publication Date:
OSTI Identifier:
20798967
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 344; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2006.03.132; PII: S0006-291X(06)00665-6; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AFFINITY; ATP; ESCHERICHIA COLI; HISTIDINE; INHIBITION; LINOLEIC ACID; LIPOSOMES; MAIZE; MITOCHONDRIA; PH VALUE; PROTEINS; RESPIRATION; SYNTHESIS

Citation Formats

Favaro, Regiane Degan, Borecky, Jiri, Colombi, Debora, and Maia, Ivan G. ZmPUMP encodes a fully functional monocot plant uncoupling mitochondrial protein whose affinity to fatty acid is increased with the introduction of a His pair at the second matrix loop. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2006.03.132.
Favaro, Regiane Degan, Borecky, Jiri, Colombi, Debora, & Maia, Ivan G. ZmPUMP encodes a fully functional monocot plant uncoupling mitochondrial protein whose affinity to fatty acid is increased with the introduction of a His pair at the second matrix loop. United States. https://doi.org/10.1016/j.bbrc.2006.03.132
Favaro, Regiane Degan, Borecky, Jiri, Colombi, Debora, and Maia, Ivan G. 2006. "ZmPUMP encodes a fully functional monocot plant uncoupling mitochondrial protein whose affinity to fatty acid is increased with the introduction of a His pair at the second matrix loop". United States. https://doi.org/10.1016/j.bbrc.2006.03.132.
@article{osti_20798967,
title = {ZmPUMP encodes a fully functional monocot plant uncoupling mitochondrial protein whose affinity to fatty acid is increased with the introduction of a His pair at the second matrix loop},
author = {Favaro, Regiane Degan and Borecky, Jiri and Colombi, Debora and Maia, Ivan G},
abstractNote = {Uncoupling proteins (UCPs) are specialized mitochondrial transporter proteins that uncouple respiration from ATP synthesis. In this study, cDNA encoding maize uncoupling protein (ZmPUMP) was expressed in Escherichia coli and recombinant ZmPUMP reconstituted in liposomes. ZmPUMP activity was associated with a linoleic acid (LA)-mediated H{sup +} efflux with K {sub m} of 56.36 {+-} 0.27 {mu}M and V {sub max} of 66.9 {mu}mol H{sup +} min{sup -1} (mg prot){sup -1}. LA-mediated H{sup +} fluxes were sensitive to ATP inhibition with K {sub i} of 2.61 {+-} 0.36 mM (at pH 7.2), a value similar to those for dicot UCPs. ZmPUMP was also used to investigate the importance of a histidine pair present in the second matrix loop of mammalian UCP1 and absent in plant UCPs. ZmPUMP with introduced His pair (Lys155His and Ala157His) displayed a 1.55-fold increase in LA-affinity while its activity remained unchanged. Our data indicate conserved properties of plant UCPs and suggest an enhancing but not essential role of the histidine pair in proton transport mechanism.},
doi = {10.1016/j.bbrc.2006.03.132},
url = {https://www.osti.gov/biblio/20798967}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 344,
place = {United States},
year = {Fri May 26 00:00:00 EDT 2006},
month = {Fri May 26 00:00:00 EDT 2006}
}