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Gene Review

PGU1  -  Pgu1p

Saccharomyces cerevisiae S288c

Synonyms: J2235, PG, PGL1, PGase SM, PSM1, ...
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Disease relevance of PGU1

  • The sequence encoding the endopolygalacturonase (PG) of Fusarium moniliforme was cloned into the E. coli/yeast shuttle vector Yepsec1 for secretion in yeast [1].
  • One of the two previously characterized genes coding for the abundant polygalacturonases I and II (PGI and PGII) found in a commercial pectinase preparation was used as a probe to isolate five more genes by screening a genomic DNA library in phage lambda EMBL4 using conditions of moderate stringency [2].

High impact information on PGU1

  • One of the MAPK-regulated genes is PGU1, which encodes a secreted enzyme that hydrolyzes polygalacturonic acid, a structural barrier to microbial invasion present in the natural plant substrate of S. cerevisiae [3].
  • A cis-acting sequence homologous to the yeast filamentation and invasion response element regulates expression of a pectinase gene from the bean pathogen Colletotrichum lindemuthianum [4].
  • In the present study, promoter deletion and mutagenesis, as well as gel shift mobility assays, allowed for the first time identification of cis-acting elements that bind protein factors and are essential for the regulation of a pectinase gene [4].
  • The signaling pathway(s) that control pectinase gene expression are currently unknown in filamentous fungi [4].
  • Disruption of tpsA only weakly reduces growth on glucose, and neither influences the glucose induction of a low affinity glucose permease nor interferes with the catabolite repression of a pectinase; it causes reduced the heat tolerance of conidia. tpsB was cloned by a polymerase chain reaction-based strategy [5].

Biological context of PGU1

  • After comparison of the current genes with their ancient (up to 35-40 million years) counterparts it was concluded that essential genes such as rRNA18S are highly conserved and that even normal 'house-keeping' genes, such as PGU1, are strikingly conserved along the millions of years that S. cerevisiae has evolved [6].
  • The expression of PGU1 gene in several strains of S. cerevisiae revealed that the polygalacturonase activity depended on the plasmid used and also on the genetic background of each strain but in all cases the enzymatic activity increased [7].
  • Mutation of the two potential glycosylation sites in PGU1 showed that the two residues individually (N318D, N330D) did not affect secreted enzyme activity, but the double mutant caused a 50% reduction in enzyme activity when compared to the wild-type PGU1 transformant [8].
  • Analysis of the aa sequence indicated that the first 25 aa constitute a signal sequence and a motif (C218XGGHGXSIGSVG230) that is usually associated with a PG active site [9].
  • Few differences were found between the two deduced amino acid sequences encoded by PGL1-1 from a pectolytic (PG+) strain (SCPP) and PGL1-2 from a non-pectolytic (PG-) strain (X2180-1B) [10].

Associations of PGU1 with chemical compounds


Other interactions of PGU1


Analytical, diagnostic and therapeutic context of PGU1

  • The time needed for wine filtration was dramatically reduced in wines elaborated with the PGU1 recombinant strain, and was comparable to the filtration time shown by wines elaborated from must supplemented with fungal pectolytic enzymes [15].
  • Cloning, sequence analysis and overexpression of a Saccharomyces cerevisiae endopolygalacturonase-encoding gene (PGL1) [10].
  • The enzyme, named Pgl1P, had an apparent M(r) of 42 kDa as shown by SDS-PAGE [14].
  • Immunoprecipitation demonstrates stable complex formation of Rad21 with Psm1 and Psm3 but not with Psc3 [16].
  • The genetic determination of polygalacturonase (PG) production in Saccharomyces cerevisiae was studied by biochemical and classical genetic techniques [17].


  1. Mutagenesis of endopolygalacturonase from Fusarium moniliforme: histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP). Caprari, C., Mattei, B., Basile, M.L., Salvi, G., Crescenzi, V., De Lorenzo, G., Cervone, F. Mol. Plant Microbe Interact. (1996) [Pubmed]
  2. The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes. Bussink, H.J., Buxton, F.P., Fraaye, B.A., de Graaff, L.H., Visser, J. Eur. J. Biochem. (1992) [Pubmed]
  3. Effectors of a developmental mitogen-activated protein kinase cascade revealed by expression signatures of signaling mutants. Madhani, H.D., Galitski, T., Lander, E.S., Fink, G.R. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  4. A cis-acting sequence homologous to the yeast filamentation and invasion response element regulates expression of a pectinase gene from the bean pathogen Colletotrichum lindemuthianum. Herbert, C., Jacquet, C., Borel, C., Esquerre-Tugaye, M.T., Dumas, B. J. Biol. Chem. (2002) [Pubmed]
  5. The filamentous fungus Aspergillus niger contains two "differentially regulated" trehalose-6-phosphate synthase-encoding genes, tpsA and tpsB. Wolschek, M.F., Kubicek, C.P. J. Biol. Chem. (1997) [Pubmed]
  6. Ancient genes of Saccharomyces cerevisiae. Veiga-Crespo, P., Poza, M., Prieto-Alcedo, M., Villa, T.G. Microbiology (Reading, Engl.) (2004) [Pubmed]
  7. Cloning, molecular characterization, and expression of an endo-polygalacturonase-encoding gene from Saccharomyces cerevisiae IM1-8b. Blanco, P., Sieiro, C., Reboredo, N.M., Villa, T.G. FEMS Microbiol. Lett. (1998) [Pubmed]
  8. Mutagenesis of key amino acids alters activity of a Saccharomyces cerevisiae endo-polygalacturonase expressed in Pichia pastoris. Blanco, P., Thow, G., Simpson, C.G., Villa, T.G., Williamson, B. FEMS Microbiol. Lett. (2002) [Pubmed]
  9. Cloning, targeted disruption and heterologous expression of the Kluyveromyces marxianus endopolygalacturonase gene (EPG1). Siekstele, R., Bartkeviciute, D., Sasnauskas, K. Yeast (1999) [Pubmed]
  10. Cloning, sequence analysis and overexpression of a Saccharomyces cerevisiae endopolygalacturonase-encoding gene (PGL1). Gognies, S., Gainvors, A., Aigle, M., Belarbi, A. Yeast (1999) [Pubmed]
  11. Engineering of an oenological Saccharomyces cerevisiae strain with pectinolytic activity and its effect on wine. Fernández-González, M., Ubeda, J.F., Cordero-Otero, R.R., Thanvanthri Gururajan, V., Briones, A.I. Int. J. Food Microbiol. (2005) [Pubmed]
  12. Regulation and role of a STE12-like transcription factor from the plant pathogen Colletotrichum lindemuthianum. Hoi, J.W., Herbert, C., Bacha, N., O'connell, R., Lafitte, C., Borderies, G., Rossignol, M., Rougé, P., Dumas, B. Mol. Microbiol. (2007) [Pubmed]
  13. Selective and sensitive detection of pectin lyase activity using a colorimetric test: application to the screening of microorganisms possessing pectin lyase activity. Nedjma, M., Hoffmann, N., Belarbi, A. Anal. Biochem. (2001) [Pubmed]
  14. Purification and characterization of acidic endo-polygalacturonase encoded by the PGL1-1 gene from Saccharomyces cerevisiae. Gainvors, A., Nedjaoum, N., Gognies, S., Muzart, M., Nedjma, M., Belarbi, A. FEMS Microbiol. Lett. (2000) [Pubmed]
  15. Use of a PGU1 recombinant Saccharomyces cerevisiae strain in oenological fermentations. Vilanova, M., Blanco, P., Cortés, S., Castro, M., Villa, T.G., Sieiro, C. J. Appl. Microbiol. (2000) [Pubmed]
  16. Characterization of fission yeast cohesin: essential anaphase proteolysis of Rad21 phosphorylated in the S phase. Tomonaga, T., Nagao, K., Kawasaki, Y., Furuya, K., Murakami, A., Morishita, J., Yuasa, T., Sutani, T., Kearsey, S.E., Uhlmann, F., Nasmyth, K., Yanagida, M. Genes Dev. (2000) [Pubmed]
  17. Genetic determination of polygalacturonase production in wild-type and laboratory strains of Saccharomyces cerevisiae. Blanco, P., Sieiro, C., Reboredo, N.M., Villa, T.G. Arch. Microbiol. (1997) [Pubmed]
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