MelampsoraV1, Main, Exploration, bibRecord, 000040

Production of small cysteine-rich effector proteins in Escherichia coli for structural and functional studies.

Identifieur interne : 000040 ( Main/Exploration ); précédent : 000039; suivant : 000041

Production of small cysteine-rich effector proteins in Escherichia coli for structural and functional studies.

Auteurs : Xiaoxiao Zhang [Australie] ; Neal Nguyen [Australie] ; Susan Breen [Australie] ; Megan A. Outram [Australie] ; Peter N. Dodds [Australie] ; Bostjan Kobe [Australie] ; Peter S. Solomon [Australie] ; Simon J. Williams [Australie]

Source :

Molecular plant pathology [ 1364-3703 ] ; 2017.

RBID : pubmed:26915457

Descripteurs français

KwdFr :
- Biochimie (méthodes), Cristallisation (MeSH), Cystéine (métabolisme), Escherichia coli (métabolisme), Nécrose (MeSH), Oxydoréduction (MeSH), Protéines Escherichia coli (biosynthèse), Protéines Escherichia coli (composition chimique), Protéines Escherichia coli (isolement et purification), Protéines recombinantes (métabolisme), Prédisposition aux maladies (MeSH), Solubilité (MeSH), Structure secondaire des protéines (MeSH), Triticum (microbiologie), Zinc (métabolisme).
MESH :
- biosynthèse : Protéines Escherichia coli.
- composition chimique : Protéines Escherichia coli.
- isolement et purification : Protéines Escherichia coli.
- microbiologie : Triticum.
- métabolisme : Cystéine, Escherichia coli, Protéines recombinantes, Zinc.
- méthodes : Biochimie.
- Cristallisation, Nécrose, Oxydoréduction, Prédisposition aux maladies, Solubilité, Structure secondaire des protéines.

English descriptors

KwdEn :
- Biochemistry (methods), Crystallization (MeSH), Cysteine (metabolism), Disease Susceptibility (MeSH), Escherichia coli (metabolism), Escherichia coli Proteins (biosynthesis), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (isolation & purification), Necrosis (MeSH), Oxidation-Reduction (MeSH), Protein Structure, Secondary (MeSH), Recombinant Proteins (metabolism), Solubility (MeSH), Triticum (microbiology), Zinc (metabolism).
MESH :
- chemical , biosynthesis : Escherichia coli Proteins.
- chemical , chemistry : Escherichia coli Proteins.
- chemical , isolation & purification : Escherichia coli Proteins.
- chemical , metabolism : Cysteine, Recombinant Proteins, Zinc.
- metabolism : Escherichia coli.
- methods : Biochemistry.
- microbiology : Triticum.
- Crystallization, Disease Susceptibility, Necrosis, Oxidation-Reduction, Protein Structure, Secondary, Solubility.

Abstract

Although the lifestyles and infection strategies of plant pathogens are diverse, a prevailing feature is the use of an arsenal of secreted proteins, known as effectors, which aid in microbial infection. In the case of eukaryotic filamentous pathogens, such as fungi and oomycetes, effector proteins are typically dissimilar, at the protein sequence level, to known protein families and functional domains. Consequently, we currently have a limited understanding of how fungal and oomycete effectors promote disease. Protein biochemistry and structural biology are two methods that can contribute greatly to the understanding of protein function. Both techniques are dependent on obtaining proteins that are pure and functional, and generally require the use of heterologous recombinant protein expression systems. Here, we present a general scheme and methodology for the production and characterization of small cysteine-rich (SCR) effectors utilizing Escherichia coli expression systems. Using this approach, we successfully produced cysteine-rich effectors derived from the biotrophic fungal pathogen Melampsora lini and the necrotrophic fungal pathogen Parastagonospora nodorum. Access to functional recombinant proteins facilitated crystallization and functional experiments. These results are discussed in the context of a general workflow that may serve as a template for others interested in understanding the function of SCR effector(s) from their plant pathogen(s) of interest.

DOI: 10.1111/mpp.12385
PubMed: 26915457
PubMed Central: PMC6638209

Affiliations:

Australie

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000050
to stream Main, to step Curation: 000050

Le document en format XML

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<front><div type="abstract" xml:lang="en">Although the lifestyles and infection strategies of plant pathogens are diverse, a prevailing feature is the use of an arsenal of secreted proteins, known as effectors, which aid in microbial infection. In the case of eukaryotic filamentous pathogens, such as fungi and oomycetes, effector proteins are typically dissimilar, at the protein sequence level, to known protein families and functional domains. Consequently, we currently have a limited understanding of how fungal and oomycete effectors promote disease. Protein biochemistry and structural biology are two methods that can contribute greatly to the understanding of protein function. Both techniques are dependent on obtaining proteins that are pure and functional, and generally require the use of heterologous recombinant protein expression systems. Here, we present a general scheme and methodology for the production and characterization of small cysteine-rich (SCR) effectors utilizing Escherichia coli expression systems. Using this approach, we successfully produced cysteine-rich effectors derived from the biotrophic fungal pathogen Melampsora lini and the necrotrophic fungal pathogen Parastagonospora nodorum. Access to functional recombinant proteins facilitated crystallization and functional experiments. These results are discussed in the context of a general workflow that may serve as a template for others interested in understanding the function of SCR effector(s) from their plant pathogen(s) of interest.</div>
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<Abstract><AbstractText>Although the lifestyles and infection strategies of plant pathogens are diverse, a prevailing feature is the use of an arsenal of secreted proteins, known as effectors, which aid in microbial infection. In the case of eukaryotic filamentous pathogens, such as fungi and oomycetes, effector proteins are typically dissimilar, at the protein sequence level, to known protein families and functional domains. Consequently, we currently have a limited understanding of how fungal and oomycete effectors promote disease. Protein biochemistry and structural biology are two methods that can contribute greatly to the understanding of protein function. Both techniques are dependent on obtaining proteins that are pure and functional, and generally require the use of heterologous recombinant protein expression systems. Here, we present a general scheme and methodology for the production and characterization of small cysteine-rich (SCR) effectors utilizing Escherichia coli expression systems. Using this approach, we successfully produced cysteine-rich effectors derived from the biotrophic fungal pathogen Melampsora lini and the necrotrophic fungal pathogen Parastagonospora nodorum. Access to functional recombinant proteins facilitated crystallization and functional experiments. These results are discussed in the context of a general workflow that may serve as a template for others interested in understanding the function of SCR effector(s) from their plant pathogen(s) of interest.</AbstractText>
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Production of small cysteine-rich effector proteins in Escherichia coli for structural and functional studies.

Production of small cysteine-rich effector proteins in Escherichia coli for structural and functional studies.

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