Disease relevance of atpE

• The Na(+)-F(1)F(0)-ATPase operon from Acetobacterium woodii. Operon structure and presence of multiple copies of atpE which encode proteolipids of 8- and 18-kda [1].
• The atpE gene product is less conserved, with 41 and 33% amino acid identity with the corresponding proteins from spinach chloroplasts and E. coli, respectively [2].
• A substitution of aspartate for glycine at residue 58 of the protein was determined by DNA sequence analysis of the uncE gene cloned from the lambda uncE106 phage DNA [3].

High impact information on atpE

• Chimeric transcripts containing the ribosome binding site of the Escherichia coli atpE gene and variants of the human structural interferon-beta gene are subject to RNase E processing in the 5'-untranslated atpE part of the transcripts [4].
• RNase E cleavage in the atpE leader region of atpE/interferon-beta hybrid transcripts in Escherichia coli causes enhanced rates of mRNA decay [4].
• The A24S uncE gene was cloned into the BamHI site of a mutant derivative of plasmid pBR322 [5].
• The segment of chromosomal DNA which codes the subunits of the FO was cloned from four independently isolated DCCD-resistant mutants, and the sequence of the subunit c gene (uncE) was determined [5].
• Linkage of the uncI gene to an efficient ribosome binding site (the translational initiation region of the uncE gene) resulted in 10-20-fold increased gene expression [6].

Chemical compound and disease context of atpE

• Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli [7].
• The transmembrane segment of cytochrome oxidase subunit III which includes the dicyclohexylcarbodiimide (DCCD)-reactive residue was very similar to E. coli uncE protein helical segment two [8].
• Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0 [9].

Biological context of atpE

• In contrast, pap-related genetic elements associated with a null phenotype either lacked homology to the papH, papC, and papD genes or displayed a restriction site polymorphism in this region [10].
• Plasmids were constructed that carried the gene for subunit c (uncE) or subunit a (uncB) behind a tac promoter [11].
• In contrast, translation of the synthetic variant atpE/synIFN-beta gene fusion is controlled by a moderately stable stem-loop structure (delta G = -4 kcal/mol; 37 degrees C) located within the coding region and overlapping the 30 S ribosomal subunit attachment site [12].
• The functional half-lives of atpE and of the other six cistrons downstream from it are similar [13].
• The bacteriophage lambda promoters, the atpE sequence, the bacteriophage fd transcriptional terminator, the f1 ORI, and the amp antibiotic resistance gene are all borne on exchangeable "modules." Thus, both the efficiency and the conditions of expression of cloned genes can be readily optimized [14].

Anatomical context of atpE

• Conversely, strains carrying mutations in the uncE gene lack the dicyclohexylcarbodiimide-binding protein but retain the 18,000-molecular-weight protein in the cell membrane [15].

Associations of atpE with chemical compounds

• The uncE408 and uncE463 mutant DNA sequences were identical and differed from normal in that a C leads to T base change occurred at nucleotide 91 of the uncE gene, resulting in leucine being replaced by phenylalanine at position 31 in the c-subunit [7].
• The uncE410 allele differs from the normal uncE gene in that C leads to T base changes occur at nucleotides 190 and 191, resulting in proline at position 64 in the c-subunit of the F1F0-ATPase being replaced by leucine [16].
• The DNA sequence of the uncE429 allele differed from normal in that a G leads to A base change occurred at nucleotide 68 of the uncE gene, resulting in glycine being replaced by aspartic acid at position 23 in the c-subunit [7].
• In contrast, translation of the uncE gene, encoding the c subunit of F0, is higher during growth on glucose than during growth on succinate [17].

Other interactions of atpE

• The affinities of binding of 30 S ribosomal subunits showed the relationship atpE greater than atpB greater than atpG [18].
• The effect of varying the temperature suggests that the secondary structure in the mRNA may affect the rate of translation initiation in the region between uncE and uncF [19].
• H2 production and H+-K+-exchange with a high Km for K+-uptake were carried out in the uncD mutant; however, both H2 production and H+-K+-exchange were lost in the Deltaunc or uncE mutant [20].

Analytical, diagnostic and therapeutic context of atpE

• The conserved Pro43 residue of the uncE protein (subunit c) of the Escherichia coli F1F0-ATPase was changed to Ser or Ala by oligonucleotide-directed mutagenesis, and the mutations were incorporated into the chromosome [9].

References