Evidence map›Paper›PMID 27507984›Full record

ArticleFrontiers in plant science2016

Crystal Structure Analysis and the Identification of Distinctive Functional Regions of the Protein Elicitor Mohrip2.

Mengjie Liu, Liangwei Duan, Meifang Wang, Hongmei Zeng, Xinqi Liu, Dewen Qiu

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Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

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6citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Mengjie LiuState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection - Chinese Academy of Agricultural Sciences Beijing, China.
Liangwei DuanState Key Laboratory of Medicinal Chemical Biology, Department of Biochemistry and Molecular Biology, College of Life Sciences, Nankai University Tianjin, China.
Meifang WangState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection - Chinese Academy of Agricultural Sciences Beijing, China.
Hongmei ZengState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection - Chinese Academy of Agricultural Sciences Beijing, China.
Xinqi LiuState Key Laboratory of Medicinal Chemical Biology, Department of Biochemistry and Molecular Biology, College of Life Sciences, Nankai University Tianjin, China.
Dewen QiuState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection - Chinese Academy of Agricultural Sciences Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein elicitor MoHrip2, which was extracted from Magnaporthe oryzae as an exocrine protein, triggers the tobacco immune system and enhances blast resistance in rice. However, the detailed mechanisms by which MoHrip2 acts as an elicitor remain unclear. Here, we investigated the structure of MoHrip2 to elucidate its functions based on molecular structure. The three-dimensional structure of MoHrip2 was obtained. Overall, the crystal structure formed a β-barrel structure and showed high similarity to the pathogenesis-related (PR) thaumatin superfamily protein thaumatin-like xylanase inhibitor (TL-XI). To investigate the functional regions responsible for MoHrip2 elicitor activities, the full length and eight truncated proteins were expressed in Escherichia coli and were evaluated for elicitor activity in tobacco. Biological function analysis showed that MoHrip2 triggered the defense system against Botrytis cinerea in tobacco. Moreover, only MoHrip2M14 and other fragments containing the 14 amino acids residues in the middle region of the protein showed the elicitor activity of inducing a hypersensitive response and resistance related pathways, which were similar to that of full-length MoHrip2. These results revealed that the central 14 amino acid residues were essential for anti-pathogenic activity.

Indexed as

crystal structuredisease resistancehypersensitive responseMoHrip2truncated mutant

Identifiers

PMID27507984
PMCPMC4960229

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