Disease relevance of dnaG

• This places the order on the E. coli genetic map at 66 min in the clockwise direction as rpsU-dnaG-rpoD which are all contained in a single macromolecular synthesis operon [1].
• Replication of phage St-1 depends on dnaG and -Z gene products, but not on dnaP function [2].
• The gene (dnaG) coding for DNA primase in the obligate intracellular parasitic bacterium, Rickettsia prowazekii, has been isolated and characterized [3].
• In addition, a multicopy dnaB recombinant, but not a multicopy dnaG recombinant, prevents the toxicity associated with this protein [4].
• A dnaG mutation of Bacillus subtilis, dnaG5, was found to be linked closely to recF [5].

High impact information on dnaG

• The rpsU-dnaG-rpoD macromolecular synthesis operon of E. coli [6].
• Here we present the nucleotide sequence of this parB region spanning 328 bp between 46% and 49% on the plasmid genome. parB is a noncoding region with extensive internal symmetry [7].
• However, our genetic data indicate that transcription from the gene L-containing operon into parB is required [7].
• Yeast DNA polymerase--DNA primase complex; cloning of PRI 1, a single essential gene related to DNA primase activity [8].
• Nucleotide sequence analysis revealed that parB cDNA has homology to glutathione S-transferase (GST; RX:glutathione R-transferase, EC 2.5.1.18) from several sources including plant and animal cells [9].

Chemical compound and disease context of dnaG

• For use as a cloning vector for Xanthomonas, a fragment containing the kanamycin resistance gene (aphA) and the stabilization locus (parB) was inserted into pXG33 [10].

Biological context of dnaG

• The nucleotide sequence of a cloned section of the Escherichia coli chromosome containing the dnaG primase gene [Lupski, J., Smiley, B., Blattner, F. & Godson, G. N. (1982) Mol. Gen, Genet. 185, 120--128] has been determined [11].
• We have characterized 24 cold-sensitive suppressor mutations of these two dnaG alleles [12].
• The complete nucleotide sequence of 5-kb DNA fragment immediately 5' to the rpsU-dnaG-rpoD macromolecular-synthesis operon in Escherichia coli has been determined [13].
• An upstream ORF overlaps 66 of the first 69 bp of the larger R. prowazekii dnaG ORF, suggesting either an overlapping gene structure or the generation of the smaller protein product of 593 aa [3].
• The regulatory regions for the rpsU-dnaG-rpoD macromolecular synthesis operon have been fused to a structural gene whose product is readily assayed (the Cmr structural gene coding for chloramphenicol acetyl transferase, CAT) [14].

Anatomical context of dnaG

• The number of flagella per unit cell length decreased sharply after shifting the culture temperature from 30 degrees to 40 degrees C in the following Ts mutants: ftsC108, ftsD1033, ftsE1181, ftsF1141, ftsG29, ftsZ84, parA110, dnaB42, nrdB, and dnaG [15].
• We have isolated an auxin-regulated cDNA, parB, from the early stage of cultured tobacco mesophyll protoplasts [9].
• Arabinosylnucleoside 5'-triphosphate inhibits DNA primase of calf thymus [16].

Associations of dnaG with chemical compounds

• The region coding for the dnaG primase has been identified by NH2-terminal and tryptic peptide amino acid analysis of the dnaG protein [11].
• Disruption of either sdgA or sdgC blocked salicylate degradation; constructs lacking sdgD accumulated gentisate [17].
• As GST, and its substrate glutathione, are shown to be related to cell proliferation as well as detoxification of xenobiotics in plant and animal cells, the role of parB is discussed in relation to the induction of proliferative activity in differentiated and nondividing mesophyll protoplasts of tobacco [9].
• In glycerol gradients, the DNA primase sedimented at a rate corresponding to a molecular mass of about 120 kDa [18].
• By deletion of the parB locus and using pBluescript KS(+) as an intermediate, pXG40 (2.8 kb), containing unique restriction sites for BamHI, EcoRI, SacI, and KpnI at the ends of the kanamycin resistance gene, was generated [10].

Other interactions of dnaG

• The three genes are in the order rpsU, dnaG rpoD, and are all encoded by the same DNA strand [19].
• Similar to dnaG and dnaT, dnaC uses several minor codons; the significance of these minor codons to the low level expression of the protein product in E. coli cells remains to be determined [20].
• A Bacillus subtilis dnaG mutant harbours a mutation in a gene homologous to the dnaN gene of Escherichia coli [5].
• Host functions directed by dnaA, so-alled dnaH, dnaI, and dnaP genes were dispensable for the viral growth [21].
• Bacillus subtilis dnaE encodes a protein homologous to DNA primase of Escherichia coli [22].

Analytical, diagnostic and therapeutic context of dnaG

• To facilitate the overexpression of Escherichia coli primase, the dnaG gene has been reconstructed using polymerase chain reaction to remove the 5' transcription terminator and the 3' RNA processing site [23].

References