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...

Descripción completa

Detalles Bibliográficos
Autores principales: Cechin, Adelmo L, Sinigaglia, Marialva, Lemke, Ney, Echeverrigaray, Sérgio, Cabrera, Odalys G, Pereira, Gonçalo AG, Mombach, José CM
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