Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola

Ueda, Mitsuhiro; Yamamoto, Norikazu; Kusuda, Mizuho; Nakazawa, Masami; Takenaka, Shigeo; Miyatake, Kazutaka; Ouchi, Kenji; Sakaguchi, Minoru; Inouye, Kuniyo

doi:10.1016/j.procbio.2012.11.005

Cited by 1 publication

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“…(Jousson et al 2004), Microsporum sp. (Jousson et al 2004), Nomuraea atypicola (Ueda et al 2013), Coccidioides posadasii (Sharpton et al 2009), Pyrenophora tritici-repentis (NCBI protein XP 001940970.1), and Arthroderma gypseum (NCBI protein XP 003173813.1). In the present study, we analyzed the phylogenetic relationship of this metalloproteinase, and described the expression of the mature proteinase of PhMEP1in Escherichia coli.…”

Section: Introductionmentioning

confidence: 99%

The Characteristic of a Novel Metalloproteinase from Puccinia Helianthi

Yang

et al. 2022

Preprint

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Objective In phytopathogenic fungi, several metalloproteinase have been implicated in virulence, but pathogenesis roles in rust are largely unknown. Here, we identified a M36 family metalloproteases from Puccina helianthi genome, designated PhMEP1, aimed to reveal the biological characteristics related to pathogenicity.Result Bioinformatics analysis showed that PhMEP1contains some of the conserved zinc-binding and active site motifs characteristics of metalloproteinase which might well be a new fungalysin-like peptidase in the M36 family. The PhMEP1 protein was over expressed as inclusion bodies in Escherichia coli. The recombinant expression products of PhMEP1 could hydrolyze azocasein and the hydrolytic activity was suppressed by metal ion chelating agents such as 1,10-phenanthroline and ethylene diamine tetraacetic acid (EDTA). The subcellular localization of PhMEP1 was detected by confocal laser scanning microscopy of the leaves from a 2-day-old Nicotiana benthamiana seedlings expressed PhMEP1-GFP fusion that showed green fluorescent protein (GFP) signal accumulated in the plasma membrane of epithelial cells.Conclusion PhMEP1 may serve as a pathogenicity factor contributing to P. helianthi penetration and infection.

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Section: Introductionmentioning

confidence: 99%

The Characteristic of a Novel Metalloproteinase from Puccinia Helianthi

Yang

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola

Cited by 1 publication

References 22 publications

The Characteristic of a Novel Metalloproteinase from Puccinia Helianthi

The Characteristic of a Novel Metalloproteinase from Puccinia Helianthi

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