funkce proteasových domén MPMV

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012789" target="_blank" >RIV/60461373:22330/04:00012789 - 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

FUNCTIONS OF PROTEASE DOMAINS IN M-PMV

Popis výsledku v původním jazyce

The role of retroviral proteases is well known. These aspartic proteases are active as homodimers and cleave Gag polyprotein precursors during particle release. M-PMV assembles immature particles in the cytoplasm and activation of the protease within theimmature particles is delayed until viral budding. Gene encoding M-PMV PR is located at the 3' end of the pro ORF. The first active form of the protease is a 17 kDa protein, containing about 50 amino acids C-terminal domain which is characteristic onlyfor betaretroviruses. Other structural elements and the overall structure of M-PMC PR are similar to other retroviral proteases1. The 17 kDa PR undergoes an autocatalytic processing from the C-terminus yielding 13 and 12 kDa proteases2. Here we have investigated the role of C-terminal domain of PR for the maturation of M-PMV. Sequences encoding the C-terminal domain of PR were deleted in the M-PMV genome and the processing of Gag polyproteins, the RT activity, and viral infectivity were

Název v anglickém jazyce

FUNCTIONS OF PROTEASE DOMAINS IN M-PMV

Popis výsledku anglicky

The role of retroviral proteases is well known. These aspartic proteases are active as homodimers and cleave Gag polyprotein precursors during particle release. M-PMV assembles immature particles in the cytoplasm and activation of the protease within theimmature particles is delayed until viral budding. Gene encoding M-PMV PR is located at the 3' end of the pro ORF. The first active form of the protease is a 17 kDa protein, containing about 50 amino acids C-terminal domain which is characteristic onlyfor betaretroviruses. Other structural elements and the overall structure of M-PMC PR are similar to other retroviral proteases1. The 17 kDa PR undergoes an autocatalytic processing from the C-terminus yielding 13 and 12 kDa proteases2. Here we have investigated the role of C-terminal domain of PR for the maturation of M-PMV. Sequences encoding the C-terminal domain of PR were deleted in the M-PMV genome and the processing of Gag polyproteins, the RT activity, and viral infectivity were

Druh

D - Stať ve sborníku

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A079" target="_blank" >LN00A079: Centrum integrované genomiky</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

The retrovirus assembly meeting

ISBN

80-86313-13-1

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

42

Název nakladatele

JPM Tisk s. r. o.

Místo vydání

Praha

Místo konání akce

Praha

Datum konání akce

1. 1. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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