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Titolo:
Chimers of two fused ADP/ATP carrier monomers indicate a single channel for ADP/ATP transport
Autore:
Huang, SG; Odoy, S; Klingenberg, M;
Indirizzi:
Univ Munich, Inst Phys Biochem, D-80336 Munich, Germany Univ Munich Munich Germany D-80336 Phys Biochem, D-80336 Munich, Germany
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 1, volume: 394, anno: 2001,
pagine: 67 - 75
SICI:
0003-9861(20011001)394:1<67:COTFAC>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADIPOSE-TISSUE MITOCHONDRIA; 6 ARGININE MUTATIONS; SACCHAROMYCES-CEREVISIAE; UNCOUPLING PROTEIN; POSITIVE RESIDUES; BINDING-PROTEIN; YEAST; DIMER; ATP; RECOMBINATION;
Keywords:
mitochondrial ADP/ATP carrier; fusion dimer protein; oxidative phosphorylation; single binding site gated pore model; kinetics of nucleotide transport;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Huang, SG Tularik Inc, 2 Corp Dr, S San Francisco, CA 94080 USA Tularik Inc 2 Corp Dr S San Francisco CA USA 94080 CA 94080 USA
Citazione:
S.G. Huang et al., "Chimers of two fused ADP/ATP carrier monomers indicate a single channel for ADP/ATP transport", ARCH BIOCH, 394(1), 2001, pp. 67-75

Abstract

The mitochondrial ADP/ATP carrier (AAC) is generally believed to function as a homodimer (Wt - Wt). It remains unknown whether the two monomers possess two independent but fully anticooperative channels or they form a singlecentral channel for nucleotide transport. Here we generated fusion proteins consisting of two tandem covalent-linked AAC monomers and studied the kinetics of ADP/ATP transport in reconstituted proteoliposomes. Functional 64-kDa fusion proteins Wt-Wt and Wt-R294A (wild-type AAC linked to a mutant having low ATP transport activity) were expressed in mitochondria of yeast transformants. Compared to homodimer Wt - Wt, the fusion protein Wt(. )Wt retained the transport activity and selectivity of ADP versus ATP. The stronglydivergent selectivities of Wt and R294A were partially propagated in the Wt-11294A fusion protein, suggesting a limited cooperativity during solute translocation. The rates of ADP or ATP transport were significantly higher than those predicted by the two-channel model. Fusion proteins for Wt-R204L (Wt linked to an inactive mutant) and R204L-Wt were not expressed in aerobically grown yeast cells, which contained plasmid rearrangements that regenerated the fully active 32-kDa homodimer Wt - Wt, suggesting that these fusion proteins are inactive in ADP/ATP transport. These results favor a singlebinding center gated pore model [Klingenberg, M. (1991) in A Study of Enzymes, Vol. 2: pp. 367-388] in which two AAC subunits cooperate for a coordinated ADP/ATP exchange through a single channel. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/01/21 alle ore 18:23:05