Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F04%3A23033143" target="_blank" >RIV/68378050:_____/04:23033143 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/04:23033143

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.

Popis výsledku v původním jazyce

Recombinant mesophilic E. coli (Ec) and thermophilic B. stearothermophilus (Bst) elongation factors EF-Tu, their isolated G-domains and six chimeric EF-Tus composed of domains of either EF-Tu were prepared and their GDP/GTP binding activities and thermostability characterized. BstEF-Tu and BstG-domain bound GDP and GTP with affinities in nanomolar and submicromolar ranges, respectively, fully comparable with those of EcEF-Tu. In contrast, the EcG-domain bound the nucleotides with much lower, micromolaraffinities. The exchange of domains 2, 3 had essentially no effect on the GDP binding activity, all complexes of chimeric EF-Tus with GDP retained Kds in the nanomolar range. The final thermostability level of either EF-Tu was the result of a cooperativeinteraction between the G-domains and domains 2+3. The G-domains set up a basic level of the thermostability, which was about 20 0C higher with the BstG-domain than with the EcG-domain.

Název v anglickém jazyce

Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.

Popis výsledku anglicky

Recombinant mesophilic E. coli (Ec) and thermophilic B. stearothermophilus (Bst) elongation factors EF-Tu, their isolated G-domains and six chimeric EF-Tus composed of domains of either EF-Tu were prepared and their GDP/GTP binding activities and thermostability characterized. BstEF-Tu and BstG-domain bound GDP and GTP with affinities in nanomolar and submicromolar ranges, respectively, fully comparable with those of EcEF-Tu. In contrast, the EcG-domain bound the nucleotides with much lower, micromolaraffinities. The exchange of domains 2, 3 had essentially no effect on the GDP binding activity, all complexes of chimeric EF-Tus with GDP retained Kds in the nanomolar range. The final thermostability level of either EF-Tu was the result of a cooperativeinteraction between the G-domains and domains 2+3. The G-domains set up a basic level of the thermostability, which was about 20 0C higher with the BstG-domain than with the EcG-domain.

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název periodika

Protein Science

ISSN

0961-8368

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

89-99

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—