Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.15 (pectinase)
 2,440 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oligodeoxyribonucleotide primers designed from the N-terminal amino acid (aa) sequence of the endopolygalacturonase (EndoPG) of Colletotrichum lindemuthianum (Cl) race beta and from an internal sequence conserved among different fungal EndoPG were used in a polymerase chain reaction (PCR) to amplify genomic related sequences of the fungus. A 542-bp fragment, designated pgA, was obtained and used as a probe to screen a partial genomic library of Cl. Among the positive clones, one was further analyzed. Nucleotide sequencing of this clone revealed on ORF encoding a 363-amino-acid (aa) polypeptide beginning with a signal peptide of 26 aa interrupted by an intron of 70 bp, and showing a high degree of homology to ten fungal EndoPG sequences. Consensus sequences were identified in the 5' non-coding region. This genomic clone was thereafter designated Clpg1. Southern analysis, performed with a Clpg1-specific probe, showed that this gene is present as a single copy in the Cl genome.
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PMID:Isolation and sequence analysis of Clpg1, a gene coding for an endopolygalacturonase of the phytopathogenic fungus Colletotrichum lindemuthianum. 862 Oct 72

Using mini-Tn5CmR::gusA, a transposon that allows transcriptional fusions to a promoterless beta-glucuronidase gene, a mutant of Erwinia carotovora subsp. carotovora SCC3193 deficient in extracellular protease production and soft-rot pathogenicity in plants was isolated. The mutant, designated SCC6004, produced normal levels of pectate lyase, polygalacturonase and cellulase. The region of the transposon insertion was partially sequenced to permit the design of specific oligonucleotide primers to amplify a 2.7 kb Clal fragment from E. carotovora subsp. carotovora SCC3193. The DNA sequence of the cloned fragment contained two complete and one partial ORFs. One of the complete ORFs (ORF1) was designated prtW and encodes a secreted protease. The deduced amino acid sequence of PrtW showed a high overall identify of 60-66% to the previously described Erwinia chrysanthemi proteases, but no homology to other proteases isolated from different E. carotovora strains. Downstream from ORF1, a further complete ORF (ORF2) and a partial ORF (ORF3) were found, with deduced peptide sequences that have significant similarity to the Inh and PrtD proteins, respectively, from E. chrysanthemi, which are involved in protease secretion. Gene fusion to the gusA reporter was employed to charaterize the regulation of prtW. The prtW gene was found to be strongly induced in the presence of plant extracts. The mutant exhibited reduced virulence, suggesting that PrtW enhances the ability of strain SCC3193 to macerate plant tissue.
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PMID:Isolation of an extracellular protease gene of Erwinia carotovora subsp. carotovora strain SCC3193 by transposon mutagenesis and the role of protease in phytopathogenicity. 1046 62

A polygalacturonase gene of Aspergillus awamori IFO 4033 was cloned by genomic Southern hybridization with a probe of a DNA fragment synthesized by PCR. This was done using primers constructed based on the N-terminal amino acid sequence of a polygalacturonase, protopectinase-AS, produced by the strain and the consensus internal amino acid sequence of fungal polygalacturonases. The cloned polygalacturonase gene, containing an ORF, encodes 362 amino acids, including a 52-bp intron. It contains the consensus nucleotide sequence of PacC binding sites, and its expression was appeared to be regulated by ambient pH. After the intron was excised, the cloned gene was inserted into an expression plasmid for yeast, pMA91, and introduced into Saccharomyces cerevisiae to be expressed. The expressed gene product was purified to a homogeneous preparation, and this confirmed that the polygalacturonase produced was the product of the cloned gene.
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PMID:Cloning and heterologous expression of gene encoding A polygalacturonase from Aspergillus awamori. 1099 42

A total of 61 S. cerevisiae strains, 60 of them isolated from wine ecosystems, were evaluated for the presence of the gene encoding endopolygalacturonase (PGU1) and for polygalacturonase (PG) activity. Nine strains lack the gene PGU1 and did not exhibit PG activity on plate assays. Of the 52 strains showing an amplified band corresponding to the size of PGU1 gene, only 36 degraded polygalacturonic acid (PGA) and 17 did not degrade it at any of the pH values used. The coding region of the PGU1 gene (ORF YJR153w) was not present in some PG activity negative strains. The S. cerevisiae UCLMS-39 strain was selected for its specific activity at different pHs, temperatures and oenological parameters. The temperature and pH optima were 50 degrees C and 3.5-5.5 respectively and it was only affected by ethanol. The PGU1 gene was cloned and sequenced. The production of a biologically functional endoPG in S. cerevisiae UCLMS-39 brings us a step closer to improving the qualities of outstanding enological yeasts naturally lacking PG activity.
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PMID:Evaluation of polygalacturonase activity in Saccharomyces cerevisiae wine strains. 1532 71

The pga1 gene encoding an endopolygalacturonase was isolated from a hyperpectinolytic mutant strain of Penicillium occitanis. It consists of an ORF of 1.155 kbp encoding a putative protein of 346 amino acids with a predicted molecular mass of 39 kDa, belonging to the family 28 of glycosyl hydrolases. The deduced amino acid sequence comprises a putative 38 N terminal amino acids of the prepropeptide. The nature and position of amino acids comprising the active site as well as the overall three-dimensional structure were well conserved between the P. occitanis pga1 and all polygalacturonases. The coding region of the pga1 gene is interrupted by three short introns of 57, 53 and 65 bp in length. In addition to the determination of the transcription start site, the promoter sequence from the pga1 gene was analysed. It showed the conservation of known response elements for CreA and Hap2-3-4 factors. Southern blot analysis at high stringency shows that the isolated polygalacturonase gene exists as a single copy in the fungus genome. Northern blot analysis confirmed the constitutive hyperpectinolytic nature of the hyperpectinolytic CT1 mutation as high levels of pga1 mRNA were observed either on pectin or on glucose-grown cells.
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PMID:Genomic organization of a polygalacturonase gene from a hyperpectinolytic mutant strain of Penicillium occitanis. 1831 39