Nicole Hugouvieux-Cotte-Pattat

Dr. Nicole Hugouvieux-Cotte-Pattat

Microbiology Adaptation & Pathogenesis(MAP), CNRS - University Lyon 1 – INSA Lyon, 69621 Villeurbanne, France
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Research Focus & Metrics

Academic Career Length

46Years (1981-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 October 1996 in Annual Review of Microbiology
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Journal Article
Closed access
Nicole Hugouvieux-Cotte-PattatNicole Hugouvieux-Cotte-Pattat
Nicole Hugouvieux-Cotte-Pattat
GCGuy Condemine
Guy Condemine
WNWilliam Nasser
William Nasser
SRSylvie Reverchon
Sylvie Reverchon
Erwinia chrysanthemi is an enterobacterium that causes various plant diseases. Its pathogenicity results from the secretion of pectinolytic enzymes responsible for the disorganization of the plant cell wall. The E. chrysanthemi strain 3937 produces two pectin methylesterases, at least seven pectate lyases, a polygalacturonase, and a pectin lyase. The extracellular degradation of the pectin leads to the formation of oligogalacturonides that are catabolized through an intracellular pathway. The pectinase genes are expressed from independent cistrons, and their transcription is favored by environmental conditions such as presence of pectin and plant extracts, stationary growth phase, low temperature, oxygen or iron limitation, and so on. Moreover, transcription of the pectin lyase gene responds to DNA-damaging agents. The differential expressions of individual pectinase genes presumably reflect their role during plant infection. The regulation of pel genes requires several regulatory systems, including the KdgR repressor, which mediates the induction of all the pectinolysis genes in the presence of pectin catabolites. KdgR also controls the genes necessary for pectinase secretion and other pectin-inducible genes not yet characterized. PecS, a cytoplasmic protein homologous to other transcriptional regulators, can bind in vitro to the regulatory regions of pectinase and cellulase genes. The PecT protein, a member of the LysR family of transcriptional regulators, represses the expression of some pectinase genes and also affects other metabolic pathways of the bacteria. Other proteins involved in global regulations, such as CRP or HNS, can bind to the regulatory regions of the pectinase genes and affect their transcription.

13 April 2014 in Environmental Microbiology Reports
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Journal Article
Open access
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Nicole Hugouvieux-Cotte-PattatNicole Hugouvieux-Cotte-Pattat
Nicole Hugouvieux-Cotte-Pattat
GCGuy Condemine
Guy Condemine
VSVladimir E. Shevchik
Vladimir E. Shevchik
Summary: Pectate lyases are enzymes involved in plant cell wall degradation. They cleave pectin using a β‐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 D ickeya 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, B acteroides 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 Y ersinia 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.

8 September 2012 in Annual Review of Phytopathology
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Journal Article
Open access
ACAmy Charkowski
Amy Charkowski
CBCarlos Blanco
Carlos Blanco
GCGuy Condemine
Guy Condemine
DEDominique Expert
Dominique Expert
TFThierry Franza
Thierry Franza
IYIris Yedidia
Iris Yedidia
Soft-rot Enterobacteriaceae (SRE), which belong to the genera Pectobacterium and Dickeya, consist mainly of broad host-range pathogens that cause wilt, rot, and blackleg diseases on a wide range of plants. They are found in plants, insects, soil, and water in agricultural regions worldwide. SRE encode all six known protein secretion systems present in gram-negative bacteria, and these systems are involved in attacking host plants and competing bacteria. They also produce and detect multiple types of small molecules to coordinate pathogenesis, modify the plant environment, attack competing microbes, and perhaps to attract insect vectors. This review integrates new information about the role protein secretion and detection and production of ions and small molecules play in soft-rot pathogenicity.

7 October 2004 in Proteomics
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Journal Article
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NKNasrin Kazemi‐Pour
Nasrin Kazemi‐Pour
GCGuy Condemine
Guy Condemine
Nicole Hugouvieux-Cotte-PattatNicole Hugouvieux-Cotte-Pattat
Nicole Hugouvieux-Cotte-Pattat

7 January 2011 in Journal of Bacteriology
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Journal Article
Open access
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JGJeremy D. Glasner
Jeremy D. Glasner
CYChing-Hong Yang
Ching-Hong Yang
SRSylvie Reverchon
Sylvie Reverchon
Nicole Hugouvieux-Cotte-PattatNicole Hugouvieux-Cotte-Pattat
Nicole Hugouvieux-Cotte-Pattat
GCGuy Condemine
Guy Condemine
NPNicole T. Perna
Nicole T. Perna
Dickeya dadantii is a plant-pathogenic enterobacterium responsible for the soft rot disease of many plants of economic importance. We present here the sequence of strain 3937, a strain widely used as a model system for research on the molecular biology and pathogenicity of this group of bacteria.

1 April 2002 in Bioorganic & Medicinal Chemistry Letters
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Journal Article
Closed access
SRSylvie Reverchon
Sylvie Reverchon
BCBernard Chantegrel
Bernard Chantegrel
CDChristian Deshayes
Christian Deshayes
ADAlain Doutheau
Alain Doutheau
Nicole Hugouvieux-Cotte-PattatNicole Hugouvieux-Cotte-Pattat
Nicole Hugouvieux-Cotte-Pattat