ATP4, the structural gene for yeast F0F1 ATPase subunit 4

Velours, Jean; Durrens, Pascal; Aigle, Michel; Guérin, Bernard

doi:10.1111/j.1432-1033.1988.tb13745.x

Cited by 49 publications

(17 citation statements)

References 39 publications

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“…Three F 1 subunits, ␣, ␤, and ⑀ were pure while ␥ and ␦ were contaminated by subunit d. Two subunits of the F 0 sector, OSCP and subunit 4, were separated ( Fig. 2A), the latter chromatographed at the end of the chromatogram because of the hydrophobicity of its N-terminal domain (32). One component ran faster than the ⑀ subunit, which is the smallest subunit of the F 1 sector ( Fig.…”

Section: Subunit H Isolation and Proteinmentioning

confidence: 99%

ATP Synthase of Yeast Mitochondria

Arselin

Vaillier

Graves

et al. 1996

Journal of Biological Chemistry

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A new subunit of the yeast ATP synthase (termed subunit h) has been isolated. Amino acid composition and N-terminal sequencing were determined by chemical methods. These data were in agreement with the sequence of the hypothetical protein L8003.20 whose primary structure was deduced from DNA sequencing of the yeast chromosome XII. The amino acid sequence encoded by ATP14 gene is 32 amino acids longer than the mature protein, which contains 92 amino acids corresponding to a calculated mass of 10,408 Da. The protein is hydrophilic and acidic with a calculated pH i of 4.08. It is not apparently related to any subunit described in other ATP synthases. A null mutant was constructed. The mutation was recessive and the mutant strain was unable to grow on glycerol medium. A high percentage of rho ؊ cells arose spontaneously. The mutant mitochondria had no detectable oligomycin-sensitive ATPase activity, but still contained ATPase activity with a catalytic sector dissociated from the membranous components. The mutant mitochondria did not contain subunit h, and the mitochondrially encoded hydrophobic subunit 6 was not present.

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Section: Subunit H Isolation and Proteinmentioning

confidence: 99%

ATP Synthase of Yeast Mitochondria

Arselin

Vaillier

Graves

et al. 1996

Journal of Biological Chemistry

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“…The mutant strains with a deletion 4⌬N-term and 4⌬TM1 were constructed according to the following strategy. NcoI sites were introduced into the ATP4 gene (24) by directed mutagenesis on single-stranded DNA (18). We used mutagenesis with T4MP5A oligonucleotide (5Ј-TATGTCTTCCATGGCAGAAAAACAGAC-3Ј) to insert a NcoI site at position 113-118 of the ATP4 gene.…”

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confidence: 99%

In the Absence of the First Membrane-spanning Segment of Subunit4(b), the Yeast ATP Synthase Is Functional but Does Not Dimerize or Oligomerize

Soubannier¹,

Vaillier

Paumard³

et al. 2002

Journal of Biological Chemistry

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The N-terminal portion of the mitochondrial b-subunit is anchored in the inner mitochondrial membrane by two hydrophobic segments. We investigated the role of the first membrane-spanning segment, which is absent in prokaryotic and chloroplastic enzymes. In the absence of the first membrane-spanning segment of the yeast subunit (subunit 4), a strong decrease in the amount of subunit g was found. The mutant ATP synthase did not dimerize or oligomerize, and mutant cells displayed anomalous mitochondrial morphologies with onion-like structures. This phenotype is similar to that of the null mutant in the ATP20 gene that encodes subunit g, a component involved in the dimerization/oligomerization of ATP synthase. Our data indicate that the first membrane-spanning segment of the mitochondrial b-subunit is not essential for the function of the enzyme since its removal did not directly alter the oxidative phosphorylation. It is proposed that the unique membrane-spanning segment of subunit g and the first membrane-spanning segment of subunit 4 interact, as shown by cross-linking experiments. We hypothesize that in eukaryotic cells the b-subunit has evolved to accommodate the interaction with the g-subunit, an associated ATP synthase component only present in the mitochondrial enzyme.

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“…F 0 is composed of a variable number of polypeptides according to the organism, ranged from three to ten. (Velours et al, 1988).…”

Section: Resultsmentioning

confidence: 99%

CHARACTERIZATION OF ATP GENE IN Calotropis procera MITOCHONDRIAL GENOME

Hassanein

2014

Egyptian Journal of Genetics and Cytology

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ATP is a substance present in all living cells that provides energy for many metabolic processes and is involved in making RNA. Most ATPases break down ATP to provide energy for molecule transport. ATP gene family provides instructions for making transporter proteins called ATPases, which carry many types of molecules, such as fats, sugars, charged atoms or molecules (ions), and drugs, across cell membranes. ATPases use energy from ATP to move substances across the cell membranes. Within ATPase, there are four subfamilies that are distinguished by their location within the cell and how they transport molecules. The F-types are located on the membranes of mitochondria, and instead of breaking down ATP to transport molecules, these types make ATPs, and so, they are called ATP synthase.ATP synthase (or complex V) is the enzyme of aerobic ATP production. It is located in the inner mitochondrial membrane of eukaryotic cells together A

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ATP4, the structural gene for yeast F₀F₁ ATPase subunit 4

Cited by 49 publications

References 39 publications

ATP Synthase of Yeast Mitochondria

ATP Synthase of Yeast Mitochondria

In the Absence of the First Membrane-spanning Segment of Subunit4(b), the Yeast ATP Synthase Is Functional but Does Not Dimerize or Oligomerize

CHARACTERIZATION OF ATP GENE IN Calotropis procera MITOCHONDRIAL GENOME

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