. "7"^^ . "Journal of molecular biology" . . . . . "The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation"@en . "Hrabal, Richard" . "\u00DAloha S-S m\u016Fstku v retrovirov\u00E9 protease a maturaci viru"@cs . . . "12"^^ . . "The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation" . . "Pichov\u00E1, Iva" . "365" . "1"^^ . . . . . "[296DF7D2B5E0]" . "P(1M0520), P(IAA4055304), Z(MSM6046137305)" . "Retroviral proteases are translated as a part of Gag-related polyproteins, and are released and activated during particle release. Mason-Pfizer monkey virus (M-PMV) Gag polyproteins assemble into immature capsids within the cytoplasmof the host cells; however, their processing occurs only after transport to the plasma membrane and subsequent release. Thus, the activity of M-PMV protease is expected to be highly regulated during the replication cycle. It has been proposed that reversible oxidation of protease cysteine residues might be responsible for such regulation. We show that cysteine residues in M-PMV protease can form an intramolecular S-S bridge. The disulfide bridge shifts the monomer/dimer equilibrium in favor of the dimer, and increases the proteolytic activity significantly. To investigate the role of this disulfide bridge in virus maturation and replication, we engineered an M-PMV clone in which both protease cysteine residues were replaced by alanine (M-PMVPRC7A/C106A). Surpr"@en . "\u00DAloha S-S m\u016Fstku v retrovirov\u00E9 protease a maturaci viru"@cs . "22330" . "RIV/60461373:22330/07:00019201!RIV08-AV0-22330___" . . "Ruml, Tom\u00E1\u0161" . "RIV/60461373:22330/07:00019201" . "0022-2836" . "The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation"@en . . . "Kluh, Ivan" . "Retroviral proteases are translated as a part of Gag-related polyproteins, and are released and activated during particle release. Mason-Pfizer monkey virus (M-PMV) Gag polyproteins assemble into immature capsids within the cytoplasmof the host cells; however, their processing occurs only after transport to the plasma membrane and subsequent release. Thus, the activity of M-PMV protease is expected to be highly regulated during the replication cycle. It has been proposed that reversible oxidation of protease cysteine residues might be responsible for such regulation. We show that cysteine residues in M-PMV protease can form an intramolecular S-S bridge. The disulfide bridge shifts the monomer/dimer equilibrium in favor of the dimer, and increases the proteolytic activity significantly. To investigate the role of this disulfide bridge in virus maturation and replication, we engineered an M-PMV clone in which both protease cysteine residues were replaced by alanine (M-PMVPRC7A/C106A). Surpr" . "1493-1504" . "T\u016Fma, Roman" . "448239" . "The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation" . . . "Svato\u0161, Ale\u0161" . "BE - Belgick\u00E9 kr\u00E1lovstv\u00ED" . "Z\u00E1bransk\u00E1, Helena" . . "retroviral protease; Mason-Pfizer monkey virus; disulfide; dimerization; maturation"@en . "Retrovirov\u00E9 proteasy jsou translatov\u00E1ny jako sou\u010D\u00E1st polyprotein\u016F Retroviral proteases are translated as a part of Gag-related polyproteins, and are released and activated during particle release. Mason-Pfizer monkey virus (M-PMV) Gag polyproteins assemble into immature capsids within the cytoplasmof the host cells; however, their processing occurs only after transport to the plasma membrane and subsequent release. Thus, the activity of M-PMV protease is expected to be highly regulated during the replication cycle. It has been proposed that reversible oxidation of protease cysteine residues might be responsible for such regulation. We show that cysteine residues in M-PMV protease can form an intramolecular S-S bridge. The disulfide bridge shifts the monomer/dimer equilibrium in favor of the dimer, and increases the proteolytic activity significantly. To investigate the role of this disulfide bridge in virus maturation and replication, we engineered an M-PMV clone in which both protease c"@cs . .