Literature DB >> 8363578

Organization and sequences of genes for the subunits of ATP synthase in the thermophilic cyanobacterium Synechococcus 6716.

H S Van Walraven1, R Lutter, J E Walker.   

Abstract

The sequences of the genes for the nine subunits of ATP synthase in the thermophilic cyanobacterium Synechococcus 6716 have been determined. The genes were identified by comparison of the encoded proteins with sequences of ATP synthase subunits in other species, and confirmed for subunits alpha, beta, delta and epsilon, by determining their N-terminal sequences. They are arranged at three separate loci. Six of them are in one cluster in the order a: c: b': b: delta: alpha, and those for the beta and epsilon subunits form a second and separate cluster. The gene for the gamma-subunit is at a third site. As in other bacteria, the gene for subunit a is immediately preceded by a gene coding for a small hydrophobic protein of unknown function, known as uncI in Escherichia coli. The gene orders in Synechococcus 6716 are related to the orders of ATP synthase genes in the plastid genomes of higher plants, and particularly of a red alga and a diatom. The sequences of the subunits are similar to those of chloroplast ATP synthase, the alpha, beta and c subunits being particularly well conserved. Differences in the primary structures of the Synechococcus 6716 and chloroplast gamma subunits probably underlie different mechanisms of activation of ATP synthase. The nucleotide sequences that are presented also contain 12 other open reading frames. One of them encodes a protein sequence related to the E. coli DNA repair enzyme, photolyase, and another codes for a protein that contains internal repeats related to sequences in the myosin heavy chain.

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Year:  1993        PMID: 8363578      PMCID: PMC1134591          DOI: 10.1042/bj2940239

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  53 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  1982-11       Impact factor: 11.205

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Journal:  J Bacteriol       Date:  1988-08       Impact factor: 3.490

4.  DNA sequence of a gene cluster coding for subunits of the F0 membrane sector of ATP synthase in Rhodospirillum rubrum. Support for modular evolution of the F1 and F0 sectors.

Authors:  G Falk; J E Walker
Journal:  Biochem J       Date:  1988-08-15       Impact factor: 3.857

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Journal:  Biochim Biophys Acta       Date:  1990-02-02

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Authors:  B Schneppe; G Deckers-Hebestreit; K Altendorf
Journal:  J Biol Chem       Date:  1990-01-05       Impact factor: 5.157

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Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

8.  Isolation, purification and characterization of the ATPase complex from the thermophilic cyanobacterium Synechococcus 6716.

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Journal:  Eur J Biochem       Date:  1983-12-01

9.  Structure-independent nucleotide sequence analysis.

Authors:  D R Mills; F R Kramer
Journal:  Proc Natl Acad Sci U S A       Date:  1979-05       Impact factor: 11.205

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Authors:  S E Curtis
Journal:  J Bacteriol       Date:  1987-01       Impact factor: 3.490

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  8 in total

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Authors:  A Das; L G Ljungdahl
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4.  The ATP synthase atpHAGDC (F1) operon from Rhodobacter capsulatus.

Authors:  R Borghese; M Crimi; L Fava; B A Melandri
Journal:  J Bacteriol       Date:  1998-01       Impact factor: 3.490

5.  Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants.

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Journal:  J Bacteriol       Date:  1994-11       Impact factor: 3.490

6.  Modulation of the proton-translocation stoichiometry of H(+)-ATP synthases in two phototrophic prokaryotes by external pH.

Authors:  B E Krenn; H S Van Walraven; M J Scholts; R Kraayenhof
Journal:  Biochem J       Date:  1993-09-15       Impact factor: 3.857

7.  Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans.

Authors:  Edgar Morales-Rios; Ian N Watt; Qifeng Zhang; Shujing Ding; Ian M Fearnley; Martin G Montgomery; Michael J O Wakelam; John E Walker
Journal:  Open Biol       Date:  2015-09       Impact factor: 6.411

8.  Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis.

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Journal:  Proc Natl Acad Sci U S A       Date:  2021-11-23       Impact factor: 11.205

  8 in total

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