Disease relevance of proA

• The corresponding gene of Enterobacter cloacae was transferred to E. coli K-12 by using RP4::mini Mu plasmid pULB113 and selecting for R-prime plasmids that carry the genes proA and proB, which are closely linked to phoE in E. coli K-12 [1].
• Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: a natural bypass of th proA step [2].
• Physical map of Salmonella typhimurium LT2 DNA in the vicinity of the proA gene [3].
• A genomic DNA library of the rumen bacterium Streptococcus bovis was constructed in Escherichia coli, and recombinant plasmids able to complement proA and proB mutations of the host were found [4].
• The hybrid plasmids pLVA(proB+A+) and pNSA(proBosm proA), were transferred into a low level osmotolerance Rhizobium fredii strain BD32 [5].

High impact information on proA

• No other proA sequences were required for toxin maturation, and excess Ca2+ prevented acylation of both lysines [6].
• Nucleotide sequence analysis of the proBA locus allowed gene assignments consistent with the NH2 and COOH-terminal analyses and amino acid compositions of homogeneous preparations of the proB and proA proteins [7].
• The stoichiometry of the oxidative phosphorylation of glutamic acid 5-semialdehyde by gamma-glutamyl phosphate reductase (glutamate semialdehyde dehydrogenase) has been established [8].
• 3. Gamma-Glutamyl phosphate reductase and 1-pyrroline-5-carboxylate reductase (EC 1.5.1.2) have mol.wts. of approx. 125000 and 190000 respectively, the specific activity of the latter being 5 X 10(3)-fold greater than either of the other two biosynthetic enzymes or of the total pathway in vivo [9].
• These results suggest that the altered gamma-glutamyl kinase results in stabilization of the complex or has an indirect effect on gamma-glutamyl phosphate reductase activity, which leads to an increase in L-proline production in Saccharomyces cerevisiae [10].

Chemical compound and disease context of proA

• Insertion element IS121 is near proA in the chromosomes of Escherichia coli K-12 strains [11].
• A DNA fragment that carried the gene (proA) encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase was cloned from the chromosomal DNA of Pseudomonas ochraceae NGJ1, and the coding region was assigned to the nucleotide sequence based on the N-terminal amino acid sequence of the enzyme purified from the organism [12].
• By selecting for growth of Escherichia coli mutant strains in the absence of the required amino acid, clones were found in a Brucella abortus library carrying genes for glutamyl phosphate reductase (proA) and beta-isopropylmalate dehydrogenase (leuB) [13].
• A simple chromatographic procedure has been devised to separate gamma-glutamyl phosphate reductase and 1-pyrroline-5-carboxylate reductase, allowing the measurement of the former in crude Escherichia coli extracts [14].

Biological context of proA

• Gamma-delta insertion mutagenesis of this subcloned fragment indicated that proB and proA genes of V. parahaemolyticus might be transcribed from different promoters [15].
• The gene dosage analysis showed that the location of the remaining operon (now called rrnH) is between metD and proA [16].
• Recombinant cosmids able to complement the thr-1, leuB, and proA mutations of the host were identified [17].
• The Pro+ recombinant cosmid restored wild-type phenotype in proA and proB but not in the proC mutants of E. coli [17].
• These tests revealed that the proBA genes of S. typhimurium form an operon, whose direction of transcription is from proB to proA [18].

Anatomical context of proA

• The proA gene encodes a typical 21-aa N-terminal signal sequence which, when fused to alkaline phosphatase by means of transposon TnphoA, was able to mediate transport of the alkaline phosphatase to the periplasm in E. coli [19].

Associations of proA with chemical compounds

• Mutants with a feedback resistant N-acetylglutamate synthase have been isolated from a proA/B, argD, argR strain by screening for proline excretion on minimal medium with arginine [20].
• Together with a proA gene described earlier, these new genes describe the major C. glutamicum proline biosynthetic pathway [2].
• However, the capacity of glutamate-gamma-semialdehyde dehydrogenase from the osmotolerant mutant to interact with the kinase was altered in thermal stability, suggesting that mutations in both proB and proA may be required for osmotolerance [21].
• While a 3.9 kb fragment which complemented proA also complemented proB, a 15 kb fragment complementing leuB could not complement other leu mutations [22].
• The hybrid plasmid pLC44-11 from the Clarke and Carbon collection, which was known to carry the proA gene, was shown also to contain the phoE gene [23].

Other interactions of proA

• More than 55 kilobases of chromosomal DNA of Salmonella typhimurium LT2, including the gpt, proA, ataA, and newD genes, were cloned in plasmid vector pULB113 [3].
• A library of Desulfovibrio desulfuricans Norway genomic DNA was constructed in Escherichia coli with pBR322 as vector and plasmids able to complement the proA and leuB mutations of the host were screened [24].
• PAI II(4787) is found between the proA and yagU at 6 min of the E. coli chromosome [25].
• E. coli W1485 putA which harbors pWFP1 carrying the proline 4-hydroxylase gene, proB74, and proA produced 25 g/l of Hyp in 96 h [26].

Analytical, diagnostic and therapeutic context of proA

• We also performed complementation tests of S. typhimurium and E. coli proB and proA mutants by using the F'128 proB and proA::Tn5 insertions [18].
• To produce the artificial bifunctional enzyme gamma-glutamyl kinase/gamma-glutamyl phosphate reductase, a mutant library of the proBA fusion gene from Bacillus subtilis was created by error-prone PCR [27].

References