dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Estadual de Campinas (UNICAMP)
dc.date.accessioned2014-05-27T11:21:52Z
dc.date.accessioned2022-10-05T18:01:34Z
dc.date.available2014-05-27T11:21:52Z
dc.date.available2022-10-05T18:01:34Z
dc.date.created2014-05-27T11:21:52Z
dc.date.issued2006-05-26
dc.identifierBiochemical and Biophysical Research Communications, v. 344, n. 1, p. 194-199, 2006.
dc.identifier0006-291X
dc.identifier1090-2104
dc.identifierhttp://hdl.handle.net/11449/68890
dc.identifier10.1016/j.bbrc.2006.03.132
dc.identifierWOS:000237408000030
dc.identifier2-s2.0-33646056397
dc.identifier8649222099176162
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3918401
dc.description.abstractUncoupling 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+ efflux with Km of 56.36 ± 0.27 μM and Vmax of 66.9 μmol H+ min-1 (mg prot)-1. LA-mediated H+ fluxes were sensitive to ATP inhibition with Ki 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. © 2006 Elsevier Inc. All rights reserved.
dc.languageeng
dc.relationBiochemical and Biophysical Research Communications
dc.relation2.559
dc.relation1,087
dc.rightsAcesso restrito
dc.sourceScopus
dc.subjectFunctional reconstitution
dc.subjectMaize
dc.subjectMitochondrial carriers
dc.subjectPlant mitochondria
dc.subjectProton transport
dc.subjectUCP
dc.subjectUncoupling mitochondrial protein
dc.subjectadenosine triphosphate
dc.subjectalanine
dc.subjectcomplementary DNA
dc.subjectfatty acid
dc.subjecthistidine
dc.subjectlinoleic acid
dc.subjectliposome
dc.subjectlysine
dc.subjectmitochondrial protein
dc.subjectcontrolled study
dc.subjectEscherichia coli
dc.subjectmammal
dc.subjectnonhuman
dc.subjectpH
dc.subjectplant
dc.subjectpriority journal
dc.subjectprotein expression
dc.subjectprotein function
dc.subjectproton transport
dc.subjectAdenosine Triphosphate
dc.subjectAmino Acid Substitution
dc.subjectCarrier Proteins
dc.subjectDNA, Complementary
dc.subjectFatty Acids
dc.subjectHistidine
dc.subjectIon Channels
dc.subjectKinetics
dc.subjectLinoleic Acid
dc.subjectLiposomes
dc.subjectMembrane Proteins
dc.subjectMitochondrial Proteins
dc.subjectMutation
dc.subjectPlant Proteins
dc.subjectProtons
dc.subjectRecombinant Proteins
dc.subjectZea mays
dc.subjectMammalia
dc.titleZmPUMP 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
dc.typeArtigo


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