Multimerizace domény p12 je nezbytná pro skládání polyproteinu Gag Mason-Pfizerova opičího viru in vitro

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F07%3A00019187" target="_blank" >RIV/60461373:22330/07:00019187 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/07:00099984

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Multimerization of the p12 domain is necessary for Mason-Pfizer monkey virus Gag assembly in vitro

Popis výsledku v původním jazyce

Mason-Pfizer monkey virus (M-PMV) Gag protein contains a domain p12 that is unique to this virus (simian retrovirus-3) and its close relatives. The ?-helical N-terminal half of p12, which contains a leucine zipper-like region, forms ordered structures inE. coli and the C-terminal half can form SDS-resistant oligomers in vitro. Together these properties suggest that p12 is a strong protein-protein interaction domain that facilitates Gag-Gag oligomerization. We have analyzed the oligomerization potentialof a panel of p12 mutants, including versions containing substituted dimer, trimer, and tetramer leucine zippers, expressed in bacteria and in the context of the Gag precursor expressed in vitro and in cells. Purified recombinant p12 and its mutants could form various oligomers as shown by chemical cross-linking experiments. Within Gag these same mutants could assemble when overexpressed in cells. In contrast, all the mutants, including the leucine zipper mutants, were assembly defectiv

Název v anglickém jazyce

Multimerization of the p12 domain is necessary for Mason-Pfizer monkey virus Gag assembly in vitro

Popis výsledku anglicky

Mason-Pfizer monkey virus (M-PMV) Gag protein contains a domain p12 that is unique to this virus (simian retrovirus-3) and its close relatives. The ?-helical N-terminal half of p12, which contains a leucine zipper-like region, forms ordered structures inE. coli and the C-terminal half can form SDS-resistant oligomers in vitro. Together these properties suggest that p12 is a strong protein-protein interaction domain that facilitates Gag-Gag oligomerization. We have analyzed the oligomerization potentialof a panel of p12 mutants, including versions containing substituted dimer, trimer, and tetramer leucine zippers, expressed in bacteria and in the context of the Gag precursor expressed in vitro and in cells. Purified recombinant p12 and its mutants could form various oligomers as shown by chemical cross-linking experiments. Within Gag these same mutants could assemble when overexpressed in cells. In contrast, all the mutants, including the leucine zipper mutants, were assembly defectiv

Druh

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

CEP obor

EE - Mikrobiologie, virologie

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

2007

Kód důvěrnosti údajů

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

Název periodika

Virology

ISSN

0042-6822

e-ISSN

—

Svazek periodika

—

Číslo periodika v rámci svazku

365

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

11

Strana od-do

260-270

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—