Disease relevance of rpoC

• Cloning and physical mapping of the Staphylococcus aureus rplL, rpoB and rpoC genes, encoding ribosomal protein L7/L12 and RNA polymerase subunits beta and beta' [1].
• Inspection of the open reading frames indicates that rpoC uses a high percentage of codons that are recognized by the major tRNA species of E. coli while ORFa and ORFb contain many codons recognized by minor tRNA species [2].
• Characterization of the rpoC gene of Streptomyces coelicolor A3(2) and its use to develop a simple and rapid method for the purification of RNA polymerase [3].
• Molecular analysis of the Haemophilus ducreyi groE heat shock operon [4].
• The groESL operon of Agrobacterium tumefaciens was cloned and sequenced and found to be highly homologous to previously analyzed groE operons in nucleotides of the coding region and in amino acid sequence [5].

High impact information on rpoC

• Over-expression of the groE operon in E. coli causes enhanced assembly of heterologously expressed ribulose bisphosphate carboxylase subunits and suppresses the heat-sensitive mutant phenotype of several dnaA alleles [6].
• We now report that multiple copies of the groE operon suppress mutations in genes encoding several diverse proteins [6].
• While the growth temperature and medium pH had little effect on inclusion body formation, co-overproduction of the dnaKJ operon, but not of the groE operon, suppressed aggregation at the expense of intracellular accumulation [7].
• Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product) [8].
• We have identified the groE+ bacterial gene product as a protein of 65,000 molecular weight [8].

Chemical compound and disease context of rpoC

• An Escherichia coli strain carrying an amber mutation (UAG) in rpoC, the gene encoding the beta prime subunit of RNA polymerase, was isolated after mutagenesis with nitrosoguanidine [9].

Biological context of rpoC

• The rpoB and rpoC mutants suggested that zwittermicin A might inhibit transcription, DNA replication, DNA gyrase or topoisomerase I; however, we found no further evidence to support any of these as the target for zwittermicin A [10].
• The results suggest that deltapsi drives zwittermicin A uptake, and that, unlike other antibiotics for which resistance maps in rpoB or rpoC, zwittermicin A does not cause the rapid cessation of DNA or RNA synthesis, suggesting a unique mechanism of antibiosis [10].
• An RNA polymerase rudder mutant rpoC (Delta 312-315) is found to suppress ppGpp deficiency phenotypes by restoring both negative and positive activities of promoter fusions in vivo, as if ppGpp were present [11].
• Four regions of symmetry, suggesting secondary structure in the mRNA, were found in the DNA sequence near the rpoC translation termination codon [2].
• The 2044 bp sequence obtained contains the distal 335 codons of rpoC followed by a 212 bp non-coding region and a second open reading frame (ORFa) of 179 codons [2].

Anatomical context of rpoC

• Characterization of the nucleotide sequence of the groE operon encoding heat shock proteins chaperone-60 and -10 of Francisella tularensis and determination of the T-cell response to the proteins in individuals vaccinated with F. tularensis [12].
• As a result of the nucleotide sequence analysis of an aphid endosymbiont's operon homologous to the Escherichia coli groE, we noted that directional base substitutions tending toward an increase of A + T content represent an obvious evolutionary trend in this prokaryotic operon, housed for a long period by an eukaryotic cell [13].

Associations of rpoC with chemical compounds

• A second class of zwittermicin A-resistant mutants was aminoglycoside sensitive and was affected in rpoB and rpoC, genes that encode subunits of RNA polymerase [10].
• Protection from dimethyl sulfate methylation was assayed at the groE promoter [14].
• This increase was present in groE and dnaK mutants but was inhibited in cells treated with chloramphenicol and novobiocin [15].

Regulatory relationships of rpoC

• A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene [16].

Other interactions of rpoC

• Probing nuclear DNA with bacterial gene probes revealed DNA fragments homologous to dnaA and rpoC genes [17].
• The htrC gene has been localized at 90 min, immediately downstream of the rpoC gene, and has been previously sequenced [18].
• The plasmid-borne reporter gene for both is lacZ (beta-galactosidase), driven by the groE promoter [19].
• We isolated novel mutations in a plasmid-borne copy of rpoC, which encodes beta', as dominant suppressors of two temperature-sensitive nusA alleles [20].
• Comparison of the structure of the groE operon with that of the endosymbiont of the aphid Acyrthosiphon pisum revealed the conservation of a sequence resembling the E. coli consensus heat shock promoter, and this sequence may be responsible for the high expression of the groEL gene in aphid endosymbionts [21].

Analytical, diagnostic and therapeutic context of rpoC

• The promoter region of the Escherichia coli groE operon was cloned using the polymerase chain reaction (PCR) [22].

References