[10] Isolation and characterization of mutants of Escherichia coli K-12 affected in oxidative phosphorylation or quinone biosynthesis

Gb, Cox; Downie, J. Allan

doi:10.1016/0076-6879(79)56013-3

Cited by 28 publications

(16 citation statements)

References 12 publications

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“…The gene described in this paper is identified as ubiG by complementation experiments and by the map position, adjacent to gyrA, provided by the sequence data. Previous attempts to isolate ubiquinone-deficient mutants have exploited the fact that such mutants are unable to grow on succinate, have low oxidase activities, and grow slowly on glucose aerobically, yet normally on glucose anaerobically (Wallace & Young, 1977a, b;Cox & Downie, 1979). In contrast to mutants defective in cytochrome d (cyd) or o (cyo) terminal oxidases, quinone mutants should also fail to grow anaerobically on certain alternative electron acceptors.…”

Section: Discussionmentioning

confidence: 99%

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Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG: Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases

Williams²,

Zamanian³

et al. 1992

Journal of General Microbiology

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We report the isolation and characterization of a mutant of Escherichia coli unable to grow aerobically on nonfermentable substrates, except for very slow growth on glycerol. The mutant contains cytochrome oxidases o and d, and grows anaerobically with alternative electron acceptors. Oxygen consumption rates of cell-free extracts were low relative to activities in an isogenic control strain, but were restored in vitro by adding ubiquinone-1 to cell-free extracts. Transformation with a cloned 2.8 kb ClaI-EcoRV fragment of chromosomal DNA restored the ability of this mutant (AN2571) to grow on succinate and also restored cellular quinone levels in this strain. The plasmid also complemented a previously isolated ubiG mutant (AN151) for aerobic growth on succinate. The nucleotide sequence revealed a 0.7kb portion of gyvA. Unidirectional nested deletions from this fragment and complementation analysis identified an open reading frame encoding a protein with a predicted molecular mass of 26-5 kDa. This gene (u6iG) encodes the enzyme 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase, which catalyses the terminal step in the biosynthesis of ubiquinone. The open reading frame is preceded by a putative Shine-Dalgarno sequence and followed by three palindromic unit sequences. Comparison of the inferred amino acid sequence of UbiG with the sequence of other S-adenosylmethionine (AdoMet)-dependent methyltransferases reveals a highly conserved AdoMet-binding region. The cloned 2.8 kb fragment also contains a sequence encoding the C-terminus of a protein with 42-44 % identity to fungal acetyl-CoA synthetases.

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Section: Discussionmentioning

confidence: 99%

“…The cells were washed twice in 0.1 M-potassium phosphate buffer (pH 7.0). After outgrowth for 5 h (about 2 generation times), cells were pelleted, washed once again in phosphate buffer and diluted at in molten SMM agar (Cox & Downie, 1979). Aliquots (4ml) were poured onto prewarmed SMM plates and incubated at 37 "C aerobically.…”

Section: Methodsmentioning

confidence: 99%

Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG: Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases

Williams²,

Zamanian³

et al. 1992

Journal of General Microbiology

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“…This motif is found in many proteins required for respiratory function (32) E. coli chromosome (1). Interestingly, three mutations that lead to respiration deficiency in E. coli had also been mapped to this region but not assigned to any open reading frame; these are ubiB, ubiD, and ubiE (33). These mutations lead to defects in ubiquinone biosynthesis that are manifested as an inability to grow on the nonfermentable carbon source, succinate.…”

Section: Tcm7mentioning

confidence: 99%

“…The E. coli ubiE mutant, AN70, is characterized by an inability to grow on nonfermentable carbon sources such as succinate and by low oxidase activities (33). Expression of the yeast COQ5 gene restores the bacterium's ability to grow with succinate as the carbon source and the succinate oxidase activity of isolated bacterial membranes.…”

Section: Figmentioning

confidence: 99%

The COQ5 Gene Encodes a Yeast Mitochondrial Protein Necessary for Ubiquinone Biosynthesis and the Assembly of the Respiratory Chain

Dibrov¹,

Robinson²,

Lemire

1997

Journal of Biological Chemistry

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Saccharomyces cerevisiae is a facultative anaerobe capable of meeting its energy requirements by fermentation and is thus an ideal system for studying the biogenesis of respiring mitochondria. We have isolated a respiration-deficient mutant exhibiting a pleiotropic loss of the mitochondrial electron transport chain. The corresponding wild-type gene, COQ5, was cloned, sequenced, and able to restore respiratory growth. Deletion of the chromosomal COQ5 gene results in a respiration deficiency and reduced levels of respiratory protein components. Exogenously added decylubiquinone can partially restore electron transport chain function to mitochondrial membranes from the deletion mutant. The COQ5 nucleotide sequence predicts a polypeptide of 307 amino acids containing a mitochondrial targeting signal. COQ5p is 43% identical to the polypeptide predicted by the Escherichia coli open reading frame, o251 (1). The COQ5 gene, when introduced into E. coli, complements the respiratory deficiency of an ubiE mutant that maps near o251, suggesting that it is the yeast homolog of the ubiE gene product. We conclude that the COQ5 gene encodes the mitochondria-localized 2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase of the yeast ubiquinone biosynthetic pathway.

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“…In addition, ubiA and ubiC map just outside the 88-to 91.5-min region (4). Ubiquinone-deficient mutants are known to grow poorly aerobically but normally anaerobically (10). However, neither the addition of menaquinone nor that of phydroxybenzoate or ubiquinone could stimulate the aerobic growth of Oxy$-12.…”

Section: Discussionmentioning

confidence: 99%

Mutations in Escherichia coli that effect sensitivity to oxygen

Jamison

Adler

1987

J Bacteriol

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[10] Isolation and characterization of mutants of Escherichia coli K-12 affected in oxidative phosphorylation or quinone biosynthesis

Cited by 28 publications

References 12 publications

Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG: Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases

Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG: Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases

The COQ5 Gene Encodes a Yeast Mitochondrial Protein Necessary for Ubiquinone Biosynthesis and the Assembly of the Respiratory Chain

Mutations in Escherichia coli that effect sensitivity to oxygen

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