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In vitro and in planta interaction evidence between Nicotiana tabacum thaumatin-like protein 1 (TLP1) and cucumber mosaic virus proteins.

Identifieur interne : 000405 ( Main/Corpus ); précédent : 000404; suivant : 000406

In vitro and in planta interaction evidence between Nicotiana tabacum thaumatin-like protein 1 (TLP1) and cucumber mosaic virus proteins.

Auteurs : Min Jung Kim ; Byung-Kook Ham ; Hwa Ran Kim ; In-Ju Lee ; Young Jin Kim ; Ki Hyun Ryu ; Young In Park ; Kyung-Hee Paek

Source :

RBID : pubmed:16307370

English descriptors

Abstract

Using a yeast two-hybrid system, we identified a plant cellular factor that interacts with the proteins of the Cucumber mosaic virus (CMV). Initially 14 candidate genes were isolated from Nicotiana tabacum, using a full-length CMV 1a gene as bait. Among the candidate genes, two were encoding thaumatin-like proteins (TLP), and were designated as Nicotiana tabacum thaumatin-like protein 1 (NtTLP1). Consistent with this observation, recombinant GST-NtTLP1 protein, which was expressed and purified in E. coli, bound tightly to CMV 1a in vitro. In planta interaction was also verified via co-immunoprecipitation. Additionally, NtTLP1 specifically interacted with the CMV movement-related proteins, movement protein and coat protein, in yeast. Real-time quantitative reverse transcription-polymerase chain reaction (RT-PCR) analysis showed that the expression of NtTLP1 increased as the result of CMV inoculation.

DOI: 10.1007/s11103-005-2619-y
PubMed: 16307370

Links to Exploration step

pubmed:16307370

Le document en format XML

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<div type="abstract" xml:lang="en">Using a yeast two-hybrid system, we identified a plant cellular factor that interacts with the proteins of the Cucumber mosaic virus (CMV). Initially 14 candidate genes were isolated from Nicotiana tabacum, using a full-length CMV 1a gene as bait. Among the candidate genes, two were encoding thaumatin-like proteins (TLP), and were designated as Nicotiana tabacum thaumatin-like protein 1 (NtTLP1). Consistent with this observation, recombinant GST-NtTLP1 protein, which was expressed and purified in E. coli, bound tightly to CMV 1a in vitro. In planta interaction was also verified via co-immunoprecipitation. Additionally, NtTLP1 specifically interacted with the CMV movement-related proteins, movement protein and coat protein, in yeast. Real-time quantitative reverse transcription-polymerase chain reaction (RT-PCR) analysis showed that the expression of NtTLP1 increased as the result of CMV inoculation.</div>
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