Source:http://linkedlifedata.com/resource/pubmed/id/20447282
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2010-5-7
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pubmed:abstractText |
Potyviral helper component-proteinase (HC-Pro) is a multifunctional protein involved in plant-virus interactions. In this study, we constructed a Carica papaya L. plant cDNA library to investigate the host factors interacting with Papaya ringspot virus (PRSV) HC-Pro using a Sos recruitment two-hybrid system (SRS). We confirmed that the full-length papaya calreticulin, designated PaCRT (GenBank accession no. FJ913889), interacts specifically with PRSV HC-Pro in yeast, in vitro and in plant cells using SRS, in vitro protein-binding assay and bimolecular fluorescent complementation assay, respectively. SRS analysis of the interaction between three PaCRT deletion mutants and PRSV HC-Pro demonstrated that the C-domain (residues 307-422), with a high Ca(2+)-binding capacity, was responsible for binding to PRSV HC-Pro. In addition, quantitative real-time reverse transcriptase-polymerase chain reaction assay showed that the expression of PaCRT mRNA was significantly upregulated in the primary stage of PRSV infection, and decreased to near-basal expression levels in noninoculated (healthy) papaya plants with virus accumulation inside host cells. PaCRT is a new calcium-binding protein that interacts with potyviral HC-Pro. It is proposed that the upregulated expression of PaCRT mRNA may be an early defence-related response to PRSV infection in the host plant, and that interaction between PRSV HC-Pro and PaCRT may be involved in plant calcium signalling pathways which could interfere with virus infection or host defence.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/HC-Pro protein, potyvirus,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1364-3703
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
335-46
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pubmed:meshHeading |
pubmed-meshheading:20447282-Amino Acid Sequence,
pubmed-meshheading:20447282-Calreticulin,
pubmed-meshheading:20447282-Carica,
pubmed-meshheading:20447282-Cysteine Endopeptidases,
pubmed-meshheading:20447282-Gene Expression Regulation, Plant,
pubmed-meshheading:20447282-Molecular Sequence Data,
pubmed-meshheading:20447282-Mutant Proteins,
pubmed-meshheading:20447282-Potyvirus,
pubmed-meshheading:20447282-Protein Binding,
pubmed-meshheading:20447282-Protein Structure, Tertiary,
pubmed-meshheading:20447282-RNA, Messenger,
pubmed-meshheading:20447282-Saccharomyces cerevisiae,
pubmed-meshheading:20447282-Sequence Alignment,
pubmed-meshheading:20447282-Two-Hybrid System Techniques,
pubmed-meshheading:20447282-Up-Regulation,
pubmed-meshheading:20447282-Viral Proteins
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pubmed:year |
2010
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pubmed:articleTitle |
Helper component-proteinase (HC-Pro) protein of Papaya ringspot virus interacts with papaya calreticulin.
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pubmed:affiliation |
Key Biotechnology Laboratory for Tropical Crops, Ministry of Agriculture, Institute of Tropical Bioscience and Biotechnology (ITBB), Chinese Academy of Tropical Agriculture Sciences (CATAS), 4 Xueyuan Road, Haikou, 571101, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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