Disease relevance of proC

• A survey of pairs of isofunctional genes from P. aeruginosa and E. coli reveals that within each pair, translated genes (including proC) have diverged more strongly than have untranslated genes specifying ribosomal or transfer RNAs [1].
• The Bradyrhizobium japonicum proline biosynthesis gene proC is essential for symbiosis [2].
• Comparison of proC and other housekeeping genes of Pseudomonas aeruginosa with their counterparts in Escherichia coli [1].
• Molecular cloning and sequence analysis of the proC gene encoding delta 1-pyrroline-5-carboxylate reductase from an extremely thermophilic eubacterium Thermus thermophilus [3].
• Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC [4].

High impact information on proC

• Analysis of these plasmids located sbcC between proC and phoR at a slightly different position from that reported before (Lloyd, R.G. and Buckman, C. 1985, J. Bacteriol. 164, 836-844) [5].
• Molecular cloning and evidence for osmoregulation of the delta 1-pyrroline-5-carboxylate reductase (proC) gene in pea (Pisum sativum L.) [6].
• Strain 1485IN carries a chromosomal inversion which corresponds to 35% of the chromosome and includes proC, trp and his genes [7].
• The proC strain elicited undeveloped nodules on soybeans that lacked nitrogen fixation activity and plant hemoglobin [2].
• Single proC mutants are auxotrophic for proline and secrete delta1-pyrroline-5-carboxylate, which are the expected phenotypes of bacterial proC mutants [8].

Chemical compound and disease context of proC

• The gene aroL in Escherichia coli K-12, specifying shikimate kinase II, was contransduced with proC at a frequency of 99% [9].
• The ampicillin resistance locus of three different ampicillin-resistant, temperature-sensitive Escherichia coli mutants was mapped between proC and purE and does not correspond to any of the known genes in this region [10].
• The mutation acrA1, leading to acriflavine sensitivity through disorganization of the plasma membrane, is located between proC and purE on the Escherichia coli K-12 chromosome [11].
• A high mutation rate at phoA, the structural gene for alkaline phosphatase, is found among N-methyl-N'-nitro-N-nitrosoguanidine-induced proC revertants of Escherichia coli [12].
• We have isolated several cDNA clones encoding delta 1-pyrroline-5-carboxylate reductase (P5CR, L-proline: NAD(P)+ 5-oxidoreductase, EC 1.5.1.2) which catalyzes the terminal step in proline biosynthesis, by direct complementation of a proC mutation in Escherichia coli with an expression library of soybean root nodule cDNA [13].

Biological context of proC

• In a comparative study of housekeeping genes of Pseudomonas aeruginosa and Escherichia coli, the nucleotide sequence of a proline biosynthetic gene, proC, of P. aeruginosa has been determined [1].
• The subunit molecular mass (approximately 29 kDa) and the N-terminal amino acid sequence of purified delta 1-pyrroline 5-carboxylate reductase, the proC gene product, were in agreement with the proC nucleotide sequence [1].
• Although it restores growth of the proC mutant, the ProDd enzyme might be detrimental to the E. coli host since the plasmid carrying the cognate proDd gene is segregated at high rate by the cells but is stabilized by small deletions which lead to a loss of the P5C reductase activity [14].
• The proC gene encoding PCA reductase of C. sticklandii was cloned, sequenced and heterologously expressed in Escherichia coli [4].
• A gene library of the extremely thermophilic bacterium, Thermus thermophilus HB27, was constructed in Escherichia coli, and recombinant plasmids able to complement proC mutants of HB27 were obtained [3].

Associations of proC with chemical compounds

• We conclude that the proC gene is essential for symbiosis and suggest that the mutant does not obtain an exogenous supply of proline in association with soybeans sufficient to satisfy its auxotrophy [2].
• Further, We showed that both LAT and pyrroline-5-carboxylate (P5C) reductase, the product of proC, were needed to convert L-Lys to L-PA in vitro [15].
• The gene was cotransducible (Pl) with intermediate-level nitrofurantoin resistance and proC [16].
• Analyses of a 12-mer and a 21-mer isolated from a cyanogen bromide digest were consistent with the proposition that the soybean P5CR isolated in these studies is very similar, although perhaps not identical, to the polypeptide predicted for the recently cloned soybean reductase (Delauney and Verma, 1990 Mol. Gen. Genet. 221, 299-305) [17].
• Pyrroline-5-carboxylate reductase (P5CR) catalyzes the reduction of Delta1-pyrroline-5-carboxylate (P5C) to proline with concomitant oxidation of NAD(P)H to NAD(P)(+) [18].

Analytical, diagnostic and therapeutic context of proC

• RT-PCR analysis indicated that proC, encoding P5CR, was expressed at the transcriptional level cultured in vitro [19].
• The structure of F13, a plasmid containing lac, purE, and proC, has been determined by heteroduplex analysis [20].
• Sequence analyses, transposon mutagenesis and expression in E. coli minicells indicate that purE and proC complementations result from the synthesis of M. smithii polypeptides with molecular weights of 36,697 and 27,836 respectively [21].
• Purification, characterization, and crystallization of human pyrroline-5-carboxylate reductase [18].

References