Disease relevance of atpB

• The atpB encodes the a [corrected] subunit of the H(+)-ATPase of E. coli [1].
• The origins in the SalI restriction fragments of 17.5 and 10.2 kilobase pairs, cloned from E. aerogenes and K. pneumoniae, respectively, were found to be between the asnA and uncB genes, as are the origins of the E. coli and Salmonella typhimurium chromosomes [2].

High impact information on atpB

• Using particle bombardment, petD-uidA transcriptional and translational fusion genes were introduced into the chloroplast genome in the large inverted repeat flanking the atpB gene [3].
• Structures of the promoters of Chlamydomonas reinhardtii plastid atpB and 16S rRNA-encoding genes were analyzed in vivo [4].
• For maximum activity, the atpB promoter requires sequences of approximately 22 base pairs upstream and approximately 60 base pairs downstream of the transcription start site [4].
• Deletion analyses of the 16S rRNA gene and atpB promoter fragments showed that the two promoters differ structurally [4].
• The papC and papD genes presumably aid in surface localization and/or polymerization of the pili-adhesin subunits and are required for expression of pili as well as of the binding properties [5].

Biological context of atpB

• Relocation of atpIB to a position in the promoter-distal region of the operon between atpG and atpD did not change the inactivation rate of atpB [6].
• The new mutant strain has a similar phenotype to the uncB mutant described previously; results from reconstitution experiments in vitro indicate that the new mutation also affects a component of the F0 portion of the Mg2+-stimulated adenosine triphosphatase [7].
• A genetic-complementation analysis, using partial diploid strains, showed that the new mutant allele, uncD409, is in a gene distinct from the other previously identified genes uncA, uncB and uncC [8].
• A comparison of the genes that were absent from the various deletion plasmids with the membrane-associated products formed after in vitro transcription-translation indicated that the uncB gene coded for the 24,000-molecular-weight protein and that the gene order was probably uncBFE [9].
• When the rbcL promoter was disrupted by a 2 bp insertion, atpB transcription decreased, whereas when the rbcL promoter region was deleted, atpB transcription increased [10].

Anatomical context of atpB

• The effects of the inhibitors dicyclohexyl-carbodiimide (DCCD), bathophenanthroline and tertiary octylcatechol, on some enzyme activities in membranes from strains of Escherichia coli carrying mutations in the uncB or uncC genes have been studied [11].
• Strains carrying mutations in the uncB gene have both the 18,000-molecular-weight protein and the dicyclohexylcarbodiimide-binding protein present in the cell membranes [9].
• Sequence analysis by the perceptron matrices (G. D. Stormo, T. D. Schneider, L. Gold, and A. Ehrenfeucht, Nucleic Acids Res. 10:2997-3011, 1982) identified a potential ribosome binding site within the uncB reading frame preceding a five-codon reading frame which is shifted one base relative to the uncB reading frame [12].
• The papD gene was sequenced, and the gene product was purified from the periplasm [13].

Associations of atpB with chemical compounds

• A sequence of 18 guanosine residues, which can impede a 3'-->5' exoribonuclease in vitro, is able to substitute for the atpB IR in vivo [14].
• Finally, a fusion of alkaline phosphatase at amino acid 271, the carboxyl-terminal residue, but not at amino acid 260, was able to complement the strain RH305 (uncB-) for growth on succinate and suggests the last 11 amino acids of the alpha subunit are critical to the function of F1F0-ATP synthase [15].
• Transcriptional and translational lacZ fusions to the promoter and to two F0 genes show that, during growth on the nonfermentable carbon source succinate, transcription of the operon and translation of uncB, encoding the a subunit of F0, are higher than during growth on glucose [16].
• S1 nuclease analysis, using the appropriate single-stranded DNA probe from this promoter region and in vivo mRNA, revealed that the 5' end of the in vivo unc mRNA initiates with a guanine residue 73 bases before the start of the proposed gene 1 or 474 bases before uncB [17].
• Oligonucleotide-directed mutagenesis was used to generate mutations in the a subunit gene (uncB) altering the glutamic acid 219 and the histidine 245 codons [18].

Regulatory relationships of atpB

• The lipophilic chelators bathophenanthroline and tertiary-octylcatechol stimulate the activity of the 'soluble' Mg-ATPase in the uncB mutant but partially inhibit the activity in the uncC mutant [11].

Other interactions of atpB

• The affinities of binding of 30 S ribosomal subunits showed the relationship atpE greater than atpB greater than atpG [19].
• The in vivo expression of uncI, the first gene of the operon, was very low, at best 10 to 20 times less than the expression of uncB [20].
• The atpB and atpF genes of Propionigenium modestum were cloned as His-tag fusion constructs and expressed in Escherichia coli [21].
• Deletion analysis by introducing mutations in the four genes in pMBR1.0 revealed that only papA and papD were required for pediocin AcH production and that the gene product of papD has both translocation and processing functions [22].

Analytical, diagnostic and therapeutic context of atpB

• The expected full-length (7-kb) transcript was recognized when RNA from the RNase E-deficient strain was subjected to Northern blot analysis with uncB- and uncC-specific probes [23].
• To examine whether these mutations affected atpB mRNA processing or accumulation in vivo, the endogenous 3' UTR was replaced with mutated sequences by biolistic transformation of Chlamydomonas chloroplasts [24].
• Cassette site-directed mutagenesis was employed to generate mutations in the a subunit (uncB (a) gene) of F1F0ATP synthase [25].

References