FUNCTIONS OF PROTEASE DOMAINS IN M-PMV

Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
FUNCTIONS OF PROTEASE DOMAINS IN M-PMV
Original language description
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
Czech name
funkce proteasových domén MPMV
Czech description
funkce proteasových domén MPMV

Project
<a href="/en/project/LN00A079" target="_blank" >LN00A079: Center of Integrated Genomics</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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