Reconstitution of purified brown adipose tissue mitochondria uncoupling protein: demonstration of separate identity of nucleotide binding and proton translocation sites by chemical probes.
AUTOR(ES)
Katiyar, S S
RESUMO
The reaction of two arginine-modifying reagents, phenylglyoxal and 2,3-butanedione, with a highly purified uncoupling protein of brown adipose tissue mitochondria decreased the GDP binding to the uncoupling protein. This inhibition was irreversible and dependent on time and concentration of the reagent. Complete inhibition of GDP binding by both reagents establishes that arginine is one of the critical amino acid residues involved in the binding of GDP. Reconstitution of the uncoupling protein (both unmodified and modified) into phospholipid vesicles by our procedure showed no effect of phenylglyoxal modification on the H+ conductance, thus demonstrating that the proton translocation site is structurally different and distinct from the GDP binding site.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=286956Documentos Relacionados
- The topology of the brown adipose tissue mitochondrial uncoupling protein determined with antibodies against its antigenic sites revealed by a library of fusion proteins.
- Molecular approach to thermogenesis in brown adipose tissue: cDNA cloning of the mitochondrial uncoupling protein.
- Sequence of the bovine mitochondrial phosphate carrier protein: structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein.
- Complete nucleotide and derived amino acid sequence of cDNA encoding the mitochondrial uncoupling protein of rat brown adipose tissue: lack of a mitochondrial targeting presequence.
- Sodium-induced calcium release from mitochondria in brown adipose tissue.
