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Název:
Expression of osmotin, an antifungal protein from Nicotiana tabacum in Escherichia coli
Autoři: Viktorová, J. ; Macková, M. ; Macek, Tomáš
Typ dokumentu: Příspěvky z konference
Konference/Akce: Biologically Active Peptides /12./, Praha (CZ), 2011-04-27 / 2011-04-29
Rok: 2011
Jazyk: eng
Abstrakt: Plants have evolved a huge variety of proteins involved in the defense against pathogens and adaptation to stressful environments. Plant proteins whose expression is strongly induced in response to infection by pathogens belong to the group of pathogenesis-related (PR) proteins. The family of PR-5 proteins constitutes a group of cysteine-rich proteins including thaumatin, zeamatin and also osmotin. Osmotin is a cationic protein of 205 residues and molecular weight of 24 kDa. It was discovered and characterized in cells of Nicotiana tabacum var. Wisconsin 38. The plasmid harbouring cDNA of osmotin from Nicotiana tabacum was constructed for transformation of Escherichia coli. The osmotin gene was prepared in fusion with histidine tail to facilitate the isolation and purification from bacterial cells. Selection of transgenic colonies was based on antibiotic resistance. The hexahistidine-tagged osmotin was overexpressed in heterologous system by using pET expression vector and purified using immobilized metal affinity chromatography. The expression of osmotin was detected and antifungal activity was tested.
Klíčová slova: antifungal activity; osmotin; pathogenesis-related proteins; recombinant protein
Číslo projektu: CEZ:AV0Z40550506 (CEP), GAP501/11/1654 (CEP)
Poskytovatel projektu: GA ČR
Zdrojový dokument: Biologically Active Peptides. 12th Conference, ISBN 978-80-86241-44-9
Instituce: Ústav organické chemie a biochemie AV ČR (web)
Informace o dostupnosti dokumentu: Dokument je dostupný v příslušném ústavu Akademie věd ČR.
Původní záznam: http://hdl.handle.net/11104/0204379
Trvalý odkaz NUŠL: http://www.nusl.cz/ntk/nusl-81034
Záznam je zařazen do těchto sbírek:
Věda a výzkum > AV ČR > Ústav organické chemie a biochemie
Konferenční materiály > Příspěvky z konference
Autoři: Viktorová, J. ; Macková, M. ; Macek, Tomáš
Typ dokumentu: Příspěvky z konference
Konference/Akce: Biologically Active Peptides /12./, Praha (CZ), 2011-04-27 / 2011-04-29
Rok: 2011
Jazyk: eng
Abstrakt: Plants have evolved a huge variety of proteins involved in the defense against pathogens and adaptation to stressful environments. Plant proteins whose expression is strongly induced in response to infection by pathogens belong to the group of pathogenesis-related (PR) proteins. The family of PR-5 proteins constitutes a group of cysteine-rich proteins including thaumatin, zeamatin and also osmotin. Osmotin is a cationic protein of 205 residues and molecular weight of 24 kDa. It was discovered and characterized in cells of Nicotiana tabacum var. Wisconsin 38. The plasmid harbouring cDNA of osmotin from Nicotiana tabacum was constructed for transformation of Escherichia coli. The osmotin gene was prepared in fusion with histidine tail to facilitate the isolation and purification from bacterial cells. Selection of transgenic colonies was based on antibiotic resistance. The hexahistidine-tagged osmotin was overexpressed in heterologous system by using pET expression vector and purified using immobilized metal affinity chromatography. The expression of osmotin was detected and antifungal activity was tested.
Klíčová slova: antifungal activity; osmotin; pathogenesis-related proteins; recombinant protein
Číslo projektu: CEZ:AV0Z40550506 (CEP), GAP501/11/1654 (CEP)
Poskytovatel projektu: GA ČR
Zdrojový dokument: Biologically Active Peptides. 12th Conference, ISBN 978-80-86241-44-9
Instituce: Ústav organické chemie a biochemie AV ČR (web)
Informace o dostupnosti dokumentu: Dokument je dostupný v příslušném ústavu Akademie věd ČR.
Původní záznam: http://hdl.handle.net/11104/0204379
Trvalý odkaz NUŠL: http://www.nusl.cz/ntk/nusl-81034
Záznam je zařazen do těchto sbírek:
Věda a výzkum > AV ČR > Ústav organické chemie a biochemie
Konferenční materiály > Příspěvky z konference
Záznam vytvořen dne 2012-01-11, naposledy upraven 2024-01-26.