"RIV/60461373:22330/04:00012789!RIV/2005/MSM/223305/N" . "The retrovirus assembly meeting" . "[23F01726930C]" . "Bauerov\u00E1, Helena" . "22330" . "Hunter, Eric" . "FUNCTIONS OF PROTEASE DOMAINS IN M-PMV" . "RIV/60461373:22330/04:00012789" . "42" . "funkce proteasov\u00FDch dom\u00E9n MPMV"@cs . "2"^^ . "Pichov\u00E1, Iva" . . "funkce proteasov\u00FDch dom\u00E9n MPMV"@cs . "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 the immature 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 only for 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 analysed. T" . "FUNCTIONS OF PROTEASE DOMAINS IN M-PMV" . "Ruml, Tom\u00E1\u0161" . "FUNCTIONS OF PROTEASE DOMAINS IN M-PMV"@en . "P(LN00A079)" . "4"^^ . "FUNCTIONS OF PROTEASE DOMAINS IN M-PMV"@en . "Praha" . "Praha" . . . . "565008" . . . . . . . "2004-01-01+01:00"^^ . . . . . "80-86313-13-1" . "JPM Tisk s. r. o." . "funkce proteasov\u00FDch dom\u00E9n MPMV"@cs . "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 the immature 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 only for 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 analysed. T"@en . . "1"^^ . . "protease;G-patch"@en .