A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels
Summary A new family of antimicrobial peptides has been discovered in Macadamia integrifolia. The first member of this new family to be purified from nut kernels was a peptide of 45 aa residues, termed MiAMP2c. This peptide inhibited various plant pathogenic fungi in vitro. cDNA clones corresponding...
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| Veröffentlicht in: | The Plant journal : for cell and molecular biology 1999-09, Vol.19 (6), p.699-710 |
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| container_title | The Plant journal : for cell and molecular biology |
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| creator | Marcus, John P. Green, Jodie L. Goulter, Ken C. Manners, John M. |
| description | Summary
A new family of antimicrobial peptides has been discovered in Macadamia integrifolia. The first member of this new family to be purified from nut kernels was a peptide of 45 aa residues, termed MiAMP2c. This peptide inhibited various plant pathogenic fungi in vitro. cDNA clones corresponding to MiAMP2c encoded a 666 aa precursor protein homologous to vicilin 7S globulin proteins. The deduced precursor protein sequence contained a putative hydrophobic N‐terminal signal sequence (28 aa), an extremely hydrophilic N‐proximal region (212 aa), and a C‐terminal region of 426 aa which is represented in all vicilins. The hydrophilic portion of the deduced protein contained the sequence for MiAMP2c as well as three additional segments having the same cysteine spacing pattern as MiAMP2c. Each member of the MiAMP2 family (i.e. MiAMP2a, b, c and d) consisted of approximately 50 amino acids and contained a C‐X‐X‐X‐C‐(10–12)X‐C‐X‐X‐X‐C motif. Sub‐ sequent isolations from seed exudates led to the purification of the predicted family members MiAMP2b and 2d, both of which also exhibited antimicrobial activity in vitro. These results suggest that some vicilins play a role in defence during seed germination. |
| doi_str_mv | 10.1046/j.1365-313x.1999.00569.x |
| format | Article |
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A new family of antimicrobial peptides has been discovered in Macadamia integrifolia. The first member of this new family to be purified from nut kernels was a peptide of 45 aa residues, termed MiAMP2c. This peptide inhibited various plant pathogenic fungi in vitro. cDNA clones corresponding to MiAMP2c encoded a 666 aa precursor protein homologous to vicilin 7S globulin proteins. The deduced precursor protein sequence contained a putative hydrophobic N‐terminal signal sequence (28 aa), an extremely hydrophilic N‐proximal region (212 aa), and a C‐terminal region of 426 aa which is represented in all vicilins. The hydrophilic portion of the deduced protein contained the sequence for MiAMP2c as well as three additional segments having the same cysteine spacing pattern as MiAMP2c. Each member of the MiAMP2 family (i.e. MiAMP2a, b, c and d) consisted of approximately 50 amino acids and contained a C‐X‐X‐X‐C‐(10–12)X‐C‐X‐X‐X‐C motif. Sub‐ sequent isolations from seed exudates led to the purification of the predicted family members MiAMP2b and 2d, both of which also exhibited antimicrobial activity in vitro. These results suggest that some vicilins play a role in defence during seed germination.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1046/j.1365-313x.1999.00569.x</identifier><identifier>PMID: 10571855</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>7S globulin protein ; Amino Acid Sequence ; Anti-Bacterial Agents ; Anti-Infective Agents - isolation & purification ; Anti-Infective Agents - metabolism ; Bacteria - drug effects ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Fungi - drug effects ; Generalities. Disease free stocks ; Genes, Plant ; Genomic Library ; globulin 7S ; Globulins - genetics ; Globulins - metabolism ; Macadamia integrifolia ; Magnoliopsida ; MiAMP2c protein ; Molecular Sequence Data ; Peptides - isolation & purification ; Peptides - metabolism ; Phytopathology. Animal pests. Plant and forest protection ; Plant Proteins - genetics ; Plant Proteins - isolation & purification ; Plant Proteins - metabolism ; Protein Processing, Post-Translational ; Seed Storage Proteins ; Seeds ; Sequence Analysis, DNA ; vicilin</subject><ispartof>The Plant journal : for cell and molecular biology, 1999-09, Vol.19 (6), p.699-710</ispartof><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4909-a298c7a99281b4820c9ddb918fe6276b9704b14e9ca6b343599bc2620319b5a3</citedby><cites>FETCH-LOGICAL-c4909-a298c7a99281b4820c9ddb918fe6276b9704b14e9ca6b343599bc2620319b5a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1365-313x.1999.00569.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-313x.1999.00569.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1193728$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10571855$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marcus, John P.</creatorcontrib><creatorcontrib>Green, Jodie L.</creatorcontrib><creatorcontrib>Goulter, Ken C.</creatorcontrib><creatorcontrib>Manners, John M.</creatorcontrib><title>A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>Summary
A new family of antimicrobial peptides has been discovered in Macadamia integrifolia. The first member of this new family to be purified from nut kernels was a peptide of 45 aa residues, termed MiAMP2c. This peptide inhibited various plant pathogenic fungi in vitro. cDNA clones corresponding to MiAMP2c encoded a 666 aa precursor protein homologous to vicilin 7S globulin proteins. The deduced precursor protein sequence contained a putative hydrophobic N‐terminal signal sequence (28 aa), an extremely hydrophilic N‐proximal region (212 aa), and a C‐terminal region of 426 aa which is represented in all vicilins. The hydrophilic portion of the deduced protein contained the sequence for MiAMP2c as well as three additional segments having the same cysteine spacing pattern as MiAMP2c. Each member of the MiAMP2 family (i.e. MiAMP2a, b, c and d) consisted of approximately 50 amino acids and contained a C‐X‐X‐X‐C‐(10–12)X‐C‐X‐X‐X‐C motif. Sub‐ sequent isolations from seed exudates led to the purification of the predicted family members MiAMP2b and 2d, both of which also exhibited antimicrobial activity in vitro. These results suggest that some vicilins play a role in defence during seed germination.</description><subject>7S globulin protein</subject><subject>Amino Acid Sequence</subject><subject>Anti-Bacterial Agents</subject><subject>Anti-Infective Agents - isolation & purification</subject><subject>Anti-Infective Agents - metabolism</subject><subject>Bacteria - drug effects</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungi - drug effects</subject><subject>Generalities. Disease free stocks</subject><subject>Genes, Plant</subject><subject>Genomic Library</subject><subject>globulin 7S</subject><subject>Globulins - genetics</subject><subject>Globulins - metabolism</subject><subject>Macadamia integrifolia</subject><subject>Magnoliopsida</subject><subject>MiAMP2c protein</subject><subject>Molecular Sequence Data</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - metabolism</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plant Proteins - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Seed Storage Proteins</subject><subject>Seeds</subject><subject>Sequence Analysis, DNA</subject><subject>vicilin</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi1ERZfCX0A-IG4J_orjkbhUVYFWRa3UPXCzbMdZeXGSJU7U3X-P010EN5BGmhnNMx-aFyFMSUmJkB-3JeWyKjjl-5ICQElIJaHcv0Cr34XvL9GKgCRFLSg7R69T2hJCay7FK3ROSVVTVVUr9HSJW9OFeMBDi00_hS64cbDBRLzzuyk0PuGQ8G4cmtn5BtvDEjufUug3zz24fsSbONg5hn6pTT77bN-MM00ebXIy-c0Y2iHm5Icfex_TG3TWmpj825O_QOvP1-urr8Xd_Zebq8u7wgkgUBgGytUGgClqhWLEQdNYoKr1ktXSQk2EpcKDM9JywSsA65hkhFOwleEX6MNxbD7s5-zTpLuQnI_R9H6Yk5bAQCgF_wTz50BxoTKojmB-U0qjb_VuDJ0ZD5oSvYijt3rRQC_i6EUc_SyO3ufWd6cds-1881fjUY0MvD8BJjkT29H0LqQ_HAVes-WET0fsKUR_-O_9ev1wmwP-CzXiq5k</recordid><startdate>199909</startdate><enddate>199909</enddate><creator>Marcus, John P.</creator><creator>Green, Jodie L.</creator><creator>Goulter, Ken C.</creator><creator>Manners, John M.</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><scope>IQODW</scope><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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199909</creationdate><title>A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels</title><author>Marcus, John P. ; Green, Jodie L. ; Goulter, Ken C. ; Manners, John M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4909-a298c7a99281b4820c9ddb918fe6276b9704b14e9ca6b343599bc2620319b5a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>7S globulin protein</topic><topic>Amino Acid Sequence</topic><topic>Anti-Bacterial Agents</topic><topic>Anti-Infective Agents - isolation & purification</topic><topic>Anti-Infective Agents - metabolism</topic><topic>Bacteria - drug effects</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungi - drug effects</topic><topic>Generalities. Disease free stocks</topic><topic>Genes, Plant</topic><topic>Genomic Library</topic><topic>globulin 7S</topic><topic>Globulins - genetics</topic><topic>Globulins - metabolism</topic><topic>Macadamia integrifolia</topic><topic>Magnoliopsida</topic><topic>MiAMP2c protein</topic><topic>Molecular Sequence Data</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - metabolism</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plant Proteins - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Seed Storage Proteins</topic><topic>Seeds</topic><topic>Sequence Analysis, DNA</topic><topic>vicilin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marcus, John P.</creatorcontrib><creatorcontrib>Green, Jodie L.</creatorcontrib><creatorcontrib>Goulter, Ken C.</creatorcontrib><creatorcontrib>Manners, John M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marcus, John P.</au><au>Green, Jodie L.</au><au>Goulter, Ken C.</au><au>Manners, John M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>1999-09</date><risdate>1999</risdate><volume>19</volume><issue>6</issue><spage>699</spage><epage>710</epage><pages>699-710</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>Summary
A new family of antimicrobial peptides has been discovered in Macadamia integrifolia. The first member of this new family to be purified from nut kernels was a peptide of 45 aa residues, termed MiAMP2c. This peptide inhibited various plant pathogenic fungi in vitro. cDNA clones corresponding to MiAMP2c encoded a 666 aa precursor protein homologous to vicilin 7S globulin proteins. The deduced precursor protein sequence contained a putative hydrophobic N‐terminal signal sequence (28 aa), an extremely hydrophilic N‐proximal region (212 aa), and a C‐terminal region of 426 aa which is represented in all vicilins. The hydrophilic portion of the deduced protein contained the sequence for MiAMP2c as well as three additional segments having the same cysteine spacing pattern as MiAMP2c. Each member of the MiAMP2 family (i.e. MiAMP2a, b, c and d) consisted of approximately 50 amino acids and contained a C‐X‐X‐X‐C‐(10–12)X‐C‐X‐X‐X‐C motif. Sub‐ sequent isolations from seed exudates led to the purification of the predicted family members MiAMP2b and 2d, both of which also exhibited antimicrobial activity in vitro. These results suggest that some vicilins play a role in defence during seed germination.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>10571855</pmid><doi>10.1046/j.1365-313x.1999.00569.x</doi><tpages>12</tpages></addata></record> |
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| ispartof | The Plant journal : for cell and molecular biology, 1999-09, Vol.19 (6), p.699-710 |
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| source | MEDLINE; Access via Wiley Online Library; IngentaConnect Free/Open Access Journals; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection) |
| subjects | 7S globulin protein Amino Acid Sequence Anti-Bacterial Agents Anti-Infective Agents - isolation & purification Anti-Infective Agents - metabolism Bacteria - drug effects Biological and medical sciences Fundamental and applied biological sciences. Psychology Fungi - drug effects Generalities. Disease free stocks Genes, Plant Genomic Library globulin 7S Globulins - genetics Globulins - metabolism Macadamia integrifolia Magnoliopsida MiAMP2c protein Molecular Sequence Data Peptides - isolation & purification Peptides - metabolism Phytopathology. Animal pests. Plant and forest protection Plant Proteins - genetics Plant Proteins - isolation & purification Plant Proteins - metabolism Protein Processing, Post-Translational Seed Storage Proteins Seeds Sequence Analysis, DNA vicilin |
| title | A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels |
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