The yeast peroxisomal adenine nucleotide transporter: characterization of two transport modes and involvement in DeltapH formation across peroxisomal membranes.
The yeast peroxisomal adenine nucleotide carrier, Ant1p, was shown to catalyse unidirectional transport in addition to exchange of substrates. In both transport modes, proton movement occurs. Nucleotide hetero-exchange is H+-compensated and electroneutral. Furthermore, microscopic fluorescence imaging of a pH-sensitive green fluorescent protein targeted to peroxisomes shows that Ant1p is involved in the formation of a DeltapH across the peroxisomal membrane, acidic inside.
Lasorsa
Francesco M
FM
Department of Pharmaco-Biology, Laboratory of Biochemistry and Molecular Biology, University of Bari, 70125 Bari, Italy.
Scarcia
Pasquale
P
Erdmann
Ralf
R
Palmieri
Ferdinando
F
Rottensteiner
Hanspeter
H
Palmieri
Luigi
L
D000227:Adenine Nucleotides / Q000378:metabolism*; D001693:Biological Transport, Active / Q000502:physiology; D003600:Cytosol / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000737:chemistry; D033704:Nucleotide Transport Proteins / Q000378:metabolism / Q000502:physiology*; D020675:Peroxisomes / Q000737:chemistry* / Q000378:metabolism; D018892:Proton-Motive Force / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism / Q000502:physiology*
C430871:ANT1 protein, S cerevisiae; D000227:Adenine Nucleotides; D033704:Nucleotide Transport Proteins; D029701:Saccharomyces cerevisiae Proteins