<i>YMC1</i>, a yeast gene encoding a new putative mitochondrial carrier protein

Graf, Roney; Baum, Bobby; Braus, Gerhard H.

doi:10.1002/yea.320090310

Cited by 15 publications

(6 citation statements)

References 19 publications

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“…Using the BLASTP program, we sought best alignments of the known IM carriers that should highlight these regions, hoping to gain insight into the function of Arg11p. We found a possibly significant relationship (five or six identities and about seven similarities (24) in 22-residue stretch) between the putative bЈ region of Arg11p and the equivalent loops of Neurospora crassa gene arg-13 (reported in the data base as an amino acid transporter) and S. cerevisiae genes YMC1 (25) and YMC2 (SWISS-PROT, accession number P38087) of unknown function (see below).…”

Section: Arg11p a New Member Of The Mitochondrial Carrier Familymentioning

confidence: 86%

The ARG11 Gene of Saccharomyces cerevisiae Encodes a Mitochondrial Integral Membrane Protein Required for Arginine Biosynthesis

Crabeel

Soetens

Rijcke

et al. 1996

Journal of Biological Chemistry

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Prototype strain MG409 (arg11-1) is a severe arginine bradytroph with greatly reduced ornithine and arginine pools, although all known enzymes required for arginine biosynthesis are functional. To identify the function required for normal arginine production impaired in MG409, we have cloned, sequenced, and performed a first molecular characterization of ARG11.We show that the ARG11 open reading frame encodes a putative 292-residue protein with a predicted molecular mass of 31.5 kDa. Sequence similarities, a tripartite organization, and six potential hydrophobic transmembrane spans suggest that Arg11p belongs to the mitochondrial integral inner membrane carrier family. We have used immuno-Western blotting and hemagglutinin epitope-tagged derivatives of Arg11p, Arg8p (a mitochondrial matrix marker), and Arg3p (a cytosolic marker) to demonstrate that Arg11p is confined to the mitochondria and behaves like an integral membrane protein.A deletion created in ARG11 causes the same arginineleaky behavior as the original arg11-1 mutation, which yields a premature stop codon at residue 266. Arg11p thus appears to fulfill a partially redundant function requiring its 27 carboxyl-terminal amino acids. As a working hypothesis, we propose that Arg11p participates in the export of matrix-made ornithine into the cytosol.

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Section: Arg11p a New Member Of The Mitochondrial Carrier Familymentioning

confidence: 86%

The ARG11 Gene of Saccharomyces cerevisiae Encodes a Mitochondrial Integral Membrane Protein Required for Arginine Biosynthesis

Crabeel

Soetens

Rijcke

et al. 1996

Journal of Biological Chemistry

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“…9a. They include two yeast mitochondrial inner membrane carrier proteins: ymc1 and ymc2 (25,26). In models of these carrier proteins, this sequence occurs in the loop between transmembrane helices 5 and 6 (Fig.…”

Section: Fig 8 Interactions Between the C-terminal Extension And Thmentioning

confidence: 99%

1.85-Å Resolution Crystal Structure of Human Ornithine Transcarbamoylase Complexed withN-Phosphonacetyl-l-ornithine

Shi

Morizono

et al. 1998

Journal of Biological Chemistry

126

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The crystal structure of human ornithine transcarbamoylase complexed with the bisubstrate analog Nphosphonacetyl-L-ornithine has been solved at 1.85-Å resolution by molecular replacement. Deleterious mutations produce clinical hyperammonia that, if untreated, results in neurological symptoms or death (ornithine transcarbamylase deficiency). The holoenzyme is trimeric, and as in other transcarbamoylases, each subunit contains an N-terminal domain that binds carbamoyl phosphate and a C-terminal domain that binds L-ornithine. The active site is located in the cleft between domains and contains additional residues from an adjacent subunit. Binding of N-phosphonacetyl-L-ornithine promotes domain closure. The resolution of the structure enables the role of active site residues in the catalytic mechanism to be critically examined. The side chain of Cys-303 is positioned so as to be able to interact with the ␦-amino group of L-ornithine which attacks the carbonyl carbon of carbamoyl phosphate in the enzymecatalyzed reaction. This sulfhydryl group forms a charge relay system with Asp-263 and the ␣-amino group of L-ornithine, instead of with His-302 and Glu-310, as previously proposed. In common with other ureotelic ornithine transcarbamoylases, the human enzyme lacks a loop of ϳ20 residues between helix H10 and ␤-strand B10 which is present in prokaryotic ornithine transcarbamoylases but has a C-terminal extension of 10 residues that interacts with the body of the protein but is exposed. The sequence of this C-terminal extension is homologous to an interhelical loop found in several membrane proteins, including mitochondrial transport proteins, suggesting a possible mode of interaction with the inner mitochondrial membrane.

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“…YMCl (AC: X67122; Graf et al, 1993) Michael Cherry, unpublished). The lower the correspond value and the higher the similarity of the two curves, the greater the probability that a particular ORF is coding.…”

Section: New Genesmentioning

confidence: 99%

Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames

Wiemann

Rechmann²,

Beneš³

et al. 1996

Yeast

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We have sequenced a region of 51 kb of the right arm from chromosome XV of Saccharomyces cerevisiae. The sequence contains 30 open reading frames (ORFs) of more than 100 amino acid residues. Thirteen new genes have been identified. Thirteen ORFs correspond to known yeast genes. One delta element and one tRNA gene were identified. Upstream of the RPO31 gene, encoding the largest subunit of RNA polymerase III, lies a Abf1p binding site. The nucleotide sequence data reported in this paper are available in the EMBL, GenBank and DDBJ nucleotide sequence databases under the Accession Number X90518.

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YMC1, a yeast gene encoding a new putative mitochondrial carrier protein

Abstract: We have cloned and sequenced a Saccharomyces cerevisiae gene coding for a protein with significant similarities to the mitochondrial carrier family. The gene we termed YMC1 (yeast mitochondrial carrier) is located on chromosome XVI, closely downstream of ARO7 encoding chorismate mutase.

Cited by 15 publications

References 19 publications

The ARG11 Gene of Saccharomyces cerevisiae Encodes a Mitochondrial Integral Membrane Protein Required for Arginine Biosynthesis

The ARG11 Gene of Saccharomyces cerevisiae Encodes a Mitochondrial Integral Membrane Protein Required for Arginine Biosynthesis

1.85-Å Resolution Crystal Structure of Human Ornithine Transcarbamoylase Complexed withN-Phosphonacetyl-l-ornithine

Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames

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