Inaktivace kolicinu Y jeho imunitním proteinem

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F08%3A00027657" target="_blank" >RIV/00216224:14310/08:00027657 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/08:00320823

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Inactivation of colicin Y by intramembrane helixhelix interaction with its immunity protein

Popis výsledku v původním jazyce

Construction of hybrids between colicins U and Y and mutagenesis of colicin Y gene (cya) revealed amino acid residues important for interactions between colicin Y and its cognate immunity protein (Cyi). Four such residues (I578, T582, Y586, and V590) were found in helices 8 and 9 of the colicin Y pore forming domain. To verify the importance of these residues, the corresponding amino acids in the colicin B protein were mutated to the residues present in colicin Y. An E. coli strain with cloned colicin Yimmunity gene (cyi) inactivated this mutant but not the wildtype colicin B. In addition, interacting amino acid pairs in Cya and Cyi were identified using a set of Cyi point mutant strains. These data are consistent with antiparallel helix-helix interactions between Cyi helix T3 and Cya helix 8 of the pore-forming domain as a molecular mechanism of colicin Y inactivation by its immunity protein.

Název v anglickém jazyce

Inactivation of colicin Y by intramembrane helixhelix interaction with its immunity protein

Popis výsledku anglicky

Construction of hybrids between colicins U and Y and mutagenesis of colicin Y gene (cya) revealed amino acid residues important for interactions between colicin Y and its cognate immunity protein (Cyi). Four such residues (I578, T582, Y586, and V590) were found in helices 8 and 9 of the colicin Y pore forming domain. To verify the importance of these residues, the corresponding amino acids in the colicin B protein were mutated to the residues present in colicin Y. An E. coli strain with cloned colicin Yimmunity gene (cyi) inactivated this mutant but not the wildtype colicin B. In addition, interacting amino acid pairs in Cya and Cyi were identified using a set of Cyi point mutant strains. These data are consistent with antiparallel helix-helix interactions between Cyi helix T3 and Cya helix 8 of the pore-forming domain as a molecular mechanism of colicin Y inactivation by its immunity protein.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

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

Název periodika

FEBS Journal

ISSN

1742-464X

e-ISSN

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Svazek periodika

275

Číslo periodika v rámci svazku

21

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

7

Strana od-do

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Kód UT WoS článku

000260010600008

EID výsledku v databázi Scopus

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