EXPRESSION OF OSMOTIN, AN ANTIFUNGAL PROTEIN FROM NICOTIANA TABACUM, IN ESCHERICHIA COLI

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F11%3A43892779" target="_blank" >RIV/60461373:22330/11:43892779 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

EXPRESSION OF OSMOTIN, AN ANTIFUNGAL PROTEIN FROM NICOTIANA TABACUM, IN ESCHERICHIA COLI

Popis výsledku v původním jazyce

Plants have involved a huge variety of proteins involved in the defense against pathogens and adaptation to stressfull environment. 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 but also osmotin. Osmotin is a cationic protein of 205 residues and a molecular weight of 24kDa. 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 theisolation 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 b

Název v anglickém jazyce

EXPRESSION OF OSMOTIN, AN ANTIFUNGAL PROTEIN FROM NICOTIANA TABACUM, IN ESCHERICHIA COLI

Popis výsledku anglicky

Plants have involved a huge variety of proteins involved in the defense against pathogens and adaptation to stressfull environment. 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 but also osmotin. Osmotin is a cationic protein of 205 residues and a molecular weight of 24kDa. 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 theisolation 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 b

Druh

D - Stať ve sborníku

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP501%2F11%2F1650" target="_blank" >GAP501/11/1650: Funkční úloha oxysterolů ve fotosynthese rostlin</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

Collection Symposium Series: Biologically Active Peptides

ISBN

978-80-86241-44-9

ISSN

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e-ISSN

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Počet stran výsledku

3

Strana od-do

151-153

Název nakladatele

Ústav organické chemie a biochemie AV ČR

Místo vydání

Praha

Místo konání akce

Praha

Datum konání akce

27. 4. 2011

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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