Bacterial pectate lyases, structural and functional diversity

被引:159
作者
Hugouvieux-Cotte-Pattat, Nicole [1 ]
Condemine, Guy
Shevchik, Vladimir E.
机构
[1] Univ Lyon 1, CNRS, UMR5240, F-69622 Villeurbanne, France
来源
ENVIRONMENTAL MICROBIOLOGY REPORTS | 2014年 / 6卷 / 05期
关键词
PARALLEL BETA-HELIX; ERWINIA-CHRYSANTHEMI; RHAMNOGALACTURONAN LYASE; CELL-WALL; BIOCHEMICAL-CHARACTERIZATION; POLYSACCHARIDE LYASES; MOLECULAR-PATTERNS; CRYSTAL-STRUCTURE; DICKEYA-DADANTII; PECTIN;
D O I
10.1111/1758-2229.12166
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
Pectate lyases are enzymes involved in plant cell wall degradation. They cleave pectin using a -elimination mechanism, specific for acidic polysaccharides. They are mainly produced by plant pathogens and plant-associated organisms, and only rarely by animals. Pectate lyases are also commonly produced in the bacterial world, either by bacteria living in close proximity with plants or by gut bacteria that find plant material in the digestive tract of their hosts. The role of pectate lyases is essential for plant pathogens, such as Dickeya dadantii, that use a set of pectate lyases as their main virulence factor. Symbiotic bacteria produce their own pectate lyases, but they also induce plant pectate lyases to initiate the symbiosis. Pectin degradation products may act as signals affecting the plant-bacteria interactions. Bacterial pectate lyases are also essential for using the pectin of dead or living plants as a carbon source for growth. In the animal gut, Bacteroides pectate lyases degrade the pectin of ingested food, and this is particularly important for herbivores that depend on their microflora for the digestion of pectin. Some human pathogens, such as Yersinia enterocolitica, produce a few intracellular pectate lyases that can facilitate their growth in the presence of highly pectinolytic bacteria, at the plant surface, in the soil or in the animal gut.
引用
收藏
页码:427 / 440
页数:14
相关论文
共 88 条
  • [1] Genome sequence of the metazoan plant-parasitic nematode Meloidogyne incognita
    Abad, Pierre
    Gouzy, Jerome
    Aury, Jean-Marc
    Castagnone-Sereno, Philippe
    Danchin, Etienne G. J.
    Deleury, Emeline
    Perfus-Barbeoch, Laetitia
    Anthouard, Veronique
    Artiguenave, Francois
    Blok, Vivian C.
    Caillaud, Marie-Cecile
    Coutinho, Pedro M.
    Dasilva, Corinne
    De Luca, Francesca
    Deau, Florence
    Esquibet, Magali
    Flutre, Timothe
    Goldstone, Jared V.
    Hamamouch, Noureddine
    Hewezi, Tarek
    Jaillon, Olivier
    Jubin, Claire
    Leonetti, Paola
    Magliano, Marc
    Maier, Tom R.
    Markov, Gabriel V.
    McVeigh, Paul
    Pesole, Graziano
    Poulain, Julie
    Robinson-Rechavi, Marc
    Sallet, Erika
    Segurens, Beatrice
    Steinbach, Delphine
    Tytgat, Tom
    Ugarte, Edgardo
    van Ghelder, Cyril
    Veronico, Pasqua
    Baum, Thomas J.
    Blaxter, Mark
    Bleve-Zacheo, Teresa
    Davis, Eric L.
    Ewbank, Jonathan J.
    Favery, Bruno
    Grenier, Eric
    Henrissat, Bernard
    Jones, John T.
    Laudet, Vincent
    Maule, Aaron G.
    Quesneville, Hadi
    Rosso, Marie-Noelle
    [J]. NATURE BIOTECHNOLOGY, 2008, 26 (08) : 909 - 915
  • [2] Structural biology of pectin degradation by Enterobacteriaceae
    Abbott, D. Wade
    Boraston, Alisdair B.
    [J]. MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2008, 72 (02) : 301 - 316
  • [3] A family 2 pectate lyase displays a rare fold and transition metal-assisted β-elimination
    Abbott, D. Wade
    Boraston, Alisdair B.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (48) : 35328 - 35336
  • [4] The Active Site of Oligogalacturonate Lyase Provides Unique Insights into Cytoplasmic Oligogalacturonate β-Elimination
    Abbott, D. Wade
    Gilbert, Harry J.
    Boraston, Alisdair B.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (50) : 39029 - 39038
  • [5] The first structure of pectate lyase belonging to polysaccharide lyase family 3
    Akita, M
    Suzuki, A
    Kobayashi, T
    Ito, S
    Yamane, T
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2001, 57 : 1786 - 1792
  • [6] Azospirillum irakense produces a novel type of pectate lyase
    Bekri, MA
    Desair, J
    Keijers, V
    Proost, P
    Searle-Van Leeuwen, M
    Vanderleyden, J
    Vande Broek, A
    [J]. JOURNAL OF BACTERIOLOGY, 1999, 181 (08) : 2440 - 2447
  • [7] The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family
    Blot, N
    Berrier, C
    Hugouvieux-Cotte-Pattat, N
    Ghazi, A
    Condemine, G
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (10) : 7936 - 7944
  • [8] Conformational and configurational features of acidic polysaccharides and their interactions with calcium ions:: a molecular modeling investigation
    Braccini, I
    Grasso, RP
    Pérez, S
    [J]. CARBOHYDRATE RESEARCH, 1999, 317 (1-4) : 119 - 130
  • [9] Brown IE, 2001, BIOCHEM J, V355, P155, DOI 10.1042/0264-6021:3550155
  • [10] The structure, function, and biosynthesis of plant cell wall pectic polysaccharides
    Caffall, Kerry Hosmer
    Mohnen, Debra
    [J]. CARBOHYDRATE RESEARCH, 2009, 344 (14) : 1879 - 1900