http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12685
Identification of a mitochondrial transporter for basic amino acids in Arabidopsis thaliana by functional reconstitution into liposomes and complementation in yeast. (Articolo in rivista)
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- Identification of a mitochondrial transporter for basic amino acids in Arabidopsis thaliana by functional reconstitution into liposomes and complementation in yeast. (Articolo in rivista) (literal)
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- 2003-01-01T00:00:00+01:00 (literal)
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Hoyos ME 1, Palmieri L 2-3, Wertin T 1, Arrigoni R 3, Polacco JC 1, Palmieri F 2. (2003)
Identification of a mitochondrial transporter for basic amino acids in Arabidopsis thaliana by functional reconstitution into liposomes and complementation in yeast.
in Plant journal (Print)
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- Hoyos ME 1, Palmieri L 2-3, Wertin T 1, Arrigoni R 3, Polacco JC 1, Palmieri F 2. (literal)
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- We describe the identification and functional characterization of two
Arabidopsis mitochondrial basic amino acid carriers (BAC), AtmBAC1 and
AtmBAC2, which are related to the yeast ornithine (Orn) carrier Ort1p, also
known as Arg11p. The arg11 mutant requires arginine (Arg) supplementation
because it fails to export sufficient ornithine from the mitochondrion to
the cytosol where it is converted to arginine. AtmBAC1 and, to a lesser
extent, AtmBAC2 partially replaced the function of Ort1p in yeast arg11. The
more efficient putative carrier, AtmBAC1, was expressed in E. coli,
purified, and reconstituted into phospholipid vesicles, where it transported
the basic l-amino acids arginine, lysine, ornithine and histidine (in order
of decreasing affinity). AtmBAC1 recognized l-histidine whereas both yeast
Ort1p and the mammalian ortholog ORNT1p do not. Also different from ORNT1p,
AtmBAC1 did not transport citrulline. AtmBAC1 appeared to be more
stereospecific than the yeast and mammalian ornithine carriers, exhibiting
greater preference for the l-forms of arginine, lysine and ornithine. By
RT-PCR, both AtmBAC1 and AtmBAC2 transcripts were detected in stems, leaves,
flowers, siliques, and seedlings. Expression of AtmBAC1 in seedlings is
consistent with its involvement in Arg breakdown in early seedling
development, i.e. delivery of Arg to mitochondrial arginase. (literal)
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- ISI Web of Science (WOS) (literal)
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- 2 Università di Bari, 3 CNR (IBBE), 1 University of Missouri (literal)
- Titolo
- Identification of a mitochondrial transporter for basic amino acids in Arabidopsis thaliana by functional reconstitution into liposomes and complementation in yeast. (literal)
- Abstract
- We describe the identification and functional characterization of two
Arabidopsis mitochondrial basic amino acid carriers (BAC), AtmBAC1 and
AtmBAC2, which are related to the yeast ornithine (Orn) carrier Ort1p, also
known as Arg11p. The arg11 mutant requires arginine (Arg) supplementation
because it fails to export sufficient ornithine from the mitochondrion to
the cytosol where it is converted to arginine. AtmBAC1 and, to a lesser
extent, AtmBAC2 partially replaced the function of Ort1p in yeast arg11. The
more efficient putative carrier, AtmBAC1, was expressed in E. coli,
purified, and reconstituted into phospholipid vesicles, where it transported
the basic l-amino acids arginine, lysine, ornithine and histidine (in order
of decreasing affinity). AtmBAC1 recognized l-histidine whereas both yeast
Ort1p and the mammalian ortholog ORNT1p do not. Also different from ORNT1p,
AtmBAC1 did not transport citrulline. AtmBAC1 appeared to be more
stereospecific than the yeast and mammalian ornithine carriers, exhibiting
greater preference for the l-forms of arginine, lysine and ornithine. By
RT-PCR, both AtmBAC1 and AtmBAC2 transcripts were detected in stems, leaves,
flowers, siliques, and seedlings. Expression of AtmBAC1 in seedlings is
consistent with its involvement in Arg breakdown in early seedling
development, i.e. delivery of Arg to mitochondrial arginase. The Km (0.19
mm) for Arg uptake by AtmBAC1 was close to the value we previously
determined for the saturable component of Arg uptake into intact
mitochondria from soybean seedling cotyledons.
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