DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, CJ | ko |
dc.contributor.author | Park, CB | ko |
dc.contributor.author | Hong, SS | ko |
dc.contributor.author | Lee, HS | ko |
dc.contributor.author | Lee, SY | ko |
dc.contributor.author | Kim, Sun-Chang | ko |
dc.date.accessioned | 2013-03-02T18:15:58Z | - |
dc.date.available | 2013-03-02T18:15:58Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-09 | - |
dc.identifier.citation | PLANT MOLECULAR BIOLOGY, v.44, no.2, pp.187 - 197 | - |
dc.identifier.issn | 0167-4412 | - |
dc.identifier.uri | http://hdl.handle.net/10203/74856 | - |
dc.description.abstract | Two novel antimicrobial peptides were isolated and characterized from the roots of shepherd's purse, Capsella bursa-pastoris. These antimicrobial peptides, named shepherin I and shepherin II, consist of 28 and 38 amino acids, respectively, and are glycine- and histidine-rich peptides. Shepherin I and shepherin II have 67.9% and 65.8% (mol/mol) glycine, respectively, and 28.6% and 21.1% (mol/mol) histidine, respectively. Both shepherins have a Gly-Gly-His motif. These antimicrobial peptides exhibit antimicrobial activity against Gram-negative bacteria and fungi. Circular dichroism spectra of shepherin I and shepherin II showed that shepherin I and shepherin II in 50% trifluoroethanol have 66.7% and 75% random coils, respectively, without any alpha -helices. cDNA sequence analysis revealed that shepherin I and shepherin II are produced from a single polypeptide, designated shep-GRP, consisting of 120 amino acids; shep-GRP has five distinct domains, an amino-terminal putative signal peptide, a shepherin I, a linker dipeptide, a shepherin II and a carboxy-terminal peptide. Southern blot analysis indicates that the gene encoding shepherins belongs to a low-complexity gene family. Northern blot analysis revealed that transcripts of shep-GRP are present in roots but not in leaves and stems. | - |
dc.language | English | - |
dc.publisher | SPRINGER | - |
dc.subject | PLANT ANTIFUNGAL PROTEINS | - |
dc.subject | MIRABILIS-JALAPA L | - |
dc.subject | DIFFERENTIAL EXPRESSION | - |
dc.subject | AMARANTHUS-CAUDATUS | - |
dc.subject | DEFENSE SYSTEM | - |
dc.subject | L SEEDS | - |
dc.subject | GENE | - |
dc.subject | PURIFICATION | - |
dc.subject | PATHOGENS | - |
dc.subject | ALFALFA | - |
dc.title | Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherds purse, Capsella bursa-pastoris. | - |
dc.type | Article | - |
dc.identifier.wosid | 000165088600007 | - |
dc.identifier.scopusid | 2-s2.0-0033674821 | - |
dc.type.rims | ART | - |
dc.citation.volume | 44 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 187 | - |
dc.citation.endingpage | 197 | - |
dc.citation.publicationname | PLANT MOLECULAR BIOLOGY | - |
dc.contributor.localauthor | Kim, Sun-Chang | - |
dc.contributor.nonIdAuthor | Park, CJ | - |
dc.contributor.nonIdAuthor | Park, CB | - |
dc.contributor.nonIdAuthor | Hong, SS | - |
dc.contributor.nonIdAuthor | Lee, HS | - |
dc.contributor.nonIdAuthor | Lee, SY | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | antimicrobial peptide | - |
dc.subject.keywordAuthor | Capsella bursa-pastoris | - |
dc.subject.keywordAuthor | glycine-rich peptide | - |
dc.subject.keywordAuthor | histidine-rich peptide | - |
dc.subject.keywordAuthor | shepherd&apos | - |
dc.subject.keywordAuthor | s purse | - |
dc.subject.keywordPlus | PLANT ANTIFUNGAL PROTEINS | - |
dc.subject.keywordPlus | MIRABILIS-JALAPA L | - |
dc.subject.keywordPlus | DIFFERENTIAL EXPRESSION | - |
dc.subject.keywordPlus | AMARANTHUS-CAUDATUS | - |
dc.subject.keywordPlus | DEFENSE SYSTEM | - |
dc.subject.keywordPlus | L SEEDS | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | PATHOGENS | - |
dc.subject.keywordPlus | ALFALFA | - |
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