Linked Life Data

9305881

Source:http://linkedlifedata.com/resource/pubmed/id/9305881

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1997-10-23
pubmed:abstractText
Potato and tomato plant uncoupling mitochondrial protein (PUMP) was reconstituted into liposomes, and K+ or H+ fluxes associated with fatty acid (FA)-induced ion movement were measured using fluorescent ion indicators potassium binding benzofuraneisophthalate and 6-methoxy-N-(3-sulfopropyl)-quinolinium. We suggest that PUMP, like its mammalian counterpart, the uncoupling protein of brown adipose tissue mitochondria (Garlid, K. D., Orosz, D. E., Modrianský, M., Vassanelli, S., and Jeek, P. (1996), J. Biol. Chem. 271, 2615-2702), allows for H+ translocation via a FA cycling mechanism. Reconstituted PUMP translocated anionic linoleic and heptylbenzoic acids, undecanesulfonate, and hexanesulfonate, but not phenylvaleric and abscisic acids or Cl-. Transport was inhibited by ATP and GDP. Internal acidification of protein-free liposomes by linoleic or heptylbenzoic acid indicated that H+ translocation occurs by FA flip-flopping across the lipid bilayer. However, addition of valinomycin after FA-initiated GDP-sensitive H+ efflux solely in proteoliposomes, indicating that influx of anionic FA via PUMP precedes a return of protonated FA carrying H+. Phenylvaleric acid, unable to flip-flop, was without effect. Kinetics of FA and undecanesulfonate uniport suggested the existence of an internal anion binding site. Exponential flux-voltage characteristics were also studied. We suggest that regulated uncoupling in plant mitochondria may be important during fruit ripening, senescence, and seed dormancy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24272-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Reconstituted plant uncoupling mitochondrial protein allows for proton translocation via fatty acid cycling mechanism.
pubmed:affiliation
Department of Membrane Transport Biophysics, Institute of Physiology, Academy of Sciences, 14220 Prague 4, Czech Republic. jezek@sun1.biomed.cas.cz
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't