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Cupin: a candidate molecular structure for the Nep1-like protein family
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....
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Published in: | BMC plant biology 2008-04, Vol.8 (1), p.50-50, Article 50 |
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description | 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.
We predict a 3d-structure for the beta-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.
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. |
doi_str_mv | 10.1186/1471-2229-8-50 |
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We predict a 3d-structure for the beta-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.
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.</description><identifier>ISSN: 1471-2229</identifier><identifier>EISSN: 1471-2229</identifier><identifier>DOI: 10.1186/1471-2229-8-50</identifier><identifier>PMID: 18447914</identifier><language>eng</language><publisher>England: BioMed Central Ltd</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Confidence Intervals ; Consensus Sequence ; Cysteine - chemistry ; Gene expression ; Genetic aspects ; Glycosylation ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Physiological aspects ; Plant diseases ; Plant Proteins - chemistry ; Protein Structure, Secondary ; Proteins ; Sequence Alignment ; Sequence Analysis, Protein</subject><ispartof>BMC plant biology, 2008-04, Vol.8 (1), p.50-50, Article 50</ispartof><rights>COPYRIGHT 2008 BioMed Central Ltd.</rights><rights>Copyright © 2008 Cechin et al; licensee BioMed Central Ltd. 2008 Cechin et al; licensee BioMed Central Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b616t-d61a09e440dac0d2280f6a2119e2540189aeab1b7097de82fa361b9eb7ed5b603</citedby><cites>FETCH-LOGICAL-b616t-d61a09e440dac0d2280f6a2119e2540189aeab1b7097de82fa361b9eb7ed5b603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2396628/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2396628/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18447914$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cechin, Adelmo L</creatorcontrib><creatorcontrib>Sinigaglia, Marialva</creatorcontrib><creatorcontrib>Lemke, Ney</creatorcontrib><creatorcontrib>Echeverrigaray, Sérgio</creatorcontrib><creatorcontrib>Cabrera, Odalys G</creatorcontrib><creatorcontrib>Pereira, Gonçalo A G</creatorcontrib><creatorcontrib>Mombach, José C M</creatorcontrib><title>Cupin: a candidate molecular structure for the Nep1-like protein family</title><title>BMC plant biology</title><addtitle>BMC Plant Biol</addtitle><description>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.
We predict a 3d-structure for the beta-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.
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.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Confidence Intervals</subject><subject>Consensus Sequence</subject><subject>Cysteine - chemistry</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>Glycosylation</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Physiological aspects</subject><subject>Plant diseases</subject><subject>Plant Proteins - chemistry</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, Protein</subject><issn>1471-2229</issn><issn>1471-2229</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNqFktuL1DAUh4so7rr66qP0SdiHrjlpmosPwjDoOrAoeHkOaXoym7VtxiQV97-3dYZ1BxFJIOGc3_mScymK50AuACR_BUxARSlVlawa8qA4vTM8vHc_KZ6kdEMICMnU4-IEJGNCATstLtfTzo-vS1NaM3a-MxnLIfRop97EMuU42TxFLF2IZb7G8gPuoOr9Nyx3MWT0Y-nM4Pvbp8UjZ_qEzw7nWfH13dsv6_fV1cfLzXp1VbUceK46DoYoZIx0xpKOUkkcNxRAIW0YAakMmhZaQZToUFJnag6twlZg17Sc1GfFZs_tgrnRu-gHE291MF7_NoS41SZmb3vUtm5qZUE5KTirW2a4o9BYgoCNU0zOrDd71m5qB-wsjjma_gh67Bn9td6GH5rWinO6AFZ7QOvDPwDHHhsGvTRFL03RUjdLQi8Pn4jh-4Qp68Eni31vRgxT0oIISYis_ysEJZWigs7Ci71wa-Yq-NGF-W07rw4Hb8OIzs_2FQjF6nkv5POjgFmT8Wfemiklvfn86Vh7gNsYUoro7rIFopeJ_Du_F_eL_Ed-GMH6F1kJ2qg</recordid><startdate>20080430</startdate><enddate>20080430</enddate><creator>Cechin, Adelmo L</creator><creator>Sinigaglia, Marialva</creator><creator>Lemke, Ney</creator><creator>Echeverrigaray, Sérgio</creator><creator>Cabrera, Odalys G</creator><creator>Pereira, Gonçalo A G</creator><creator>Mombach, José C M</creator><general>BioMed Central Ltd</general><general>BioMed Central</general><general>BMC</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20080430</creationdate><title>Cupin: a candidate molecular structure for the Nep1-like protein family</title><author>Cechin, Adelmo L ; Sinigaglia, Marialva ; Lemke, Ney ; Echeverrigaray, Sérgio ; Cabrera, Odalys G ; Pereira, Gonçalo A G ; Mombach, José C M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b616t-d61a09e440dac0d2280f6a2119e2540189aeab1b7097de82fa361b9eb7ed5b603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Confidence Intervals</topic><topic>Consensus Sequence</topic><topic>Cysteine - chemistry</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>Glycosylation</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Physiological aspects</topic><topic>Plant diseases</topic><topic>Plant Proteins - chemistry</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, Protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cechin, Adelmo L</creatorcontrib><creatorcontrib>Sinigaglia, Marialva</creatorcontrib><creatorcontrib>Lemke, Ney</creatorcontrib><creatorcontrib>Echeverrigaray, Sérgio</creatorcontrib><creatorcontrib>Cabrera, Odalys G</creatorcontrib><creatorcontrib>Pereira, Gonçalo A G</creatorcontrib><creatorcontrib>Mombach, José C M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>BMC plant biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cechin, Adelmo L</au><au>Sinigaglia, Marialva</au><au>Lemke, Ney</au><au>Echeverrigaray, Sérgio</au><au>Cabrera, Odalys G</au><au>Pereira, Gonçalo A G</au><au>Mombach, José C M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cupin: a candidate molecular structure for the Nep1-like protein family</atitle><jtitle>BMC plant biology</jtitle><addtitle>BMC Plant Biol</addtitle><date>2008-04-30</date><risdate>2008</risdate><volume>8</volume><issue>1</issue><spage>50</spage><epage>50</epage><pages>50-50</pages><artnum>50</artnum><issn>1471-2229</issn><eissn>1471-2229</eissn><abstract>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.
We predict a 3d-structure for the beta-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.
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.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>18447914</pmid><doi>10.1186/1471-2229-8-50</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Motifs Amino Acid Sequence Confidence Intervals Consensus Sequence Cysteine - chemistry Gene expression Genetic aspects Glycosylation Models, Molecular Molecular Sequence Data Molecular Structure Physiological aspects Plant diseases Plant Proteins - chemistry Protein Structure, Secondary Proteins Sequence Alignment Sequence Analysis, Protein |
title | Cupin: a candidate molecular structure for the Nep1-like protein family |
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