Cargando…
Cupin: A candidate molecular structure for the Nep1-like protein family
BACKGROUND: NEP1-like proteins (NLPs) are a novel family of microbial elicitors of plant necrosis. Some NLPs induce a hypersensitive-like response in dicot plants though the basis for this response remains unclear. In addition, the spatial structure and the role of these highly conserved proteins ar...
Autores principales: | , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2396628/ https://www.ncbi.nlm.nih.gov/pubmed/18447914 http://dx.doi.org/10.1186/1471-2229-8-50 |
_version_ | 1782155579812216832 |
---|---|
author | Cechin, Adelmo L Sinigaglia, Marialva Lemke, Ney Echeverrigaray, Sérgio Cabrera, Odalys G Pereira, Gonçalo AG Mombach, José CM |
author_facet | Cechin, Adelmo L Sinigaglia, Marialva Lemke, Ney Echeverrigaray, Sérgio Cabrera, Odalys G Pereira, Gonçalo AG Mombach, José CM |
author_sort | Cechin, Adelmo L |
collection | PubMed |
description | BACKGROUND: NEP1-like proteins (NLPs) are a novel family of microbial elicitors of plant necrosis. Some NLPs induce a hypersensitive-like response in dicot plants though the basis for this response remains unclear. In addition, the spatial structure and the role of these highly conserved proteins are not known. RESULTS: We predict a 3d-structure for the β-rich section of the NLPs based on alignments, prediction tools and molecular dynamics. We calculated a consensus sequence from 42 NLPs proteins, predicted its secondary structure and obtained a high quality alignment of this structure and conserved residues with the two Cupin superfamily motifs. The conserved sequence GHRHDWE and several common residues, especially some conserved histidines, in NLPs match closely the two cupin motifs. Besides other common residues shared by dicot Auxin-Binding Proteins (ABPs) and NLPs, an additional conserved histidine found in all dicot ABPs was also found in all NLPs at the same position. CONCLUSION: We propose that the necrosis inducing protein class belongs to the Cupin superfamily. Based on the 3d-structure, we are proposing some possible functions for the NLPs. |
format | Text |
id | pubmed-2396628 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-23966282008-05-28 Cupin: A candidate molecular structure for the Nep1-like protein family Cechin, Adelmo L Sinigaglia, Marialva Lemke, Ney Echeverrigaray, Sérgio Cabrera, Odalys G Pereira, Gonçalo AG Mombach, José CM BMC Plant Biol Research Article BACKGROUND: NEP1-like proteins (NLPs) are a novel family of microbial elicitors of plant necrosis. Some NLPs induce a hypersensitive-like response in dicot plants though the basis for this response remains unclear. In addition, the spatial structure and the role of these highly conserved proteins are not known. RESULTS: We predict a 3d-structure for the β-rich section of the NLPs based on alignments, prediction tools and molecular dynamics. We calculated a consensus sequence from 42 NLPs proteins, predicted its secondary structure and obtained a high quality alignment of this structure and conserved residues with the two Cupin superfamily motifs. The conserved sequence GHRHDWE and several common residues, especially some conserved histidines, in NLPs match closely the two cupin motifs. Besides other common residues shared by dicot Auxin-Binding Proteins (ABPs) and NLPs, an additional conserved histidine found in all dicot ABPs was also found in all NLPs at the same position. CONCLUSION: We propose that the necrosis inducing protein class belongs to the Cupin superfamily. Based on the 3d-structure, we are proposing some possible functions for the NLPs. BioMed Central 2008-04-30 /pmc/articles/PMC2396628/ /pubmed/18447914 http://dx.doi.org/10.1186/1471-2229-8-50 Text en Copyright © 2008 Cechin et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Cechin, Adelmo L Sinigaglia, Marialva Lemke, Ney Echeverrigaray, Sérgio Cabrera, Odalys G Pereira, Gonçalo AG Mombach, José CM Cupin: A candidate molecular structure for the Nep1-like protein family |
title | Cupin: A candidate molecular structure for the Nep1-like protein family |
title_full | Cupin: A candidate molecular structure for the Nep1-like protein family |
title_fullStr | Cupin: A candidate molecular structure for the Nep1-like protein family |
title_full_unstemmed | Cupin: A candidate molecular structure for the Nep1-like protein family |
title_short | Cupin: A candidate molecular structure for the Nep1-like protein family |
title_sort | cupin: a candidate molecular structure for the nep1-like protein family |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2396628/ https://www.ncbi.nlm.nih.gov/pubmed/18447914 http://dx.doi.org/10.1186/1471-2229-8-50 |
work_keys_str_mv | AT cechinadelmol cupinacandidatemolecularstructureforthenep1likeproteinfamily AT sinigagliamarialva cupinacandidatemolecularstructureforthenep1likeproteinfamily AT lemkeney cupinacandidatemolecularstructureforthenep1likeproteinfamily AT echeverrigaraysergio cupinacandidatemolecularstructureforthenep1likeproteinfamily AT cabreraodalysg cupinacandidatemolecularstructureforthenep1likeproteinfamily AT pereiragoncaloag cupinacandidatemolecularstructureforthenep1likeproteinfamily AT mombachjosecm cupinacandidatemolecularstructureforthenep1likeproteinfamily |