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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F07%3A00019201%21RIV08-AV0-22330___
rdf:type
n13:Vysledek skos:Concept
dcterms:description
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 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 Retrovirové proteasy jsou translatovány jako součást polyproteinů 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
dcterms:title
Úloha S-S můstku v retrovirové protease a maturaci viru The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation
skos:prefLabel
The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation Úloha S-S můstku v retrovirové protease a maturaci viru The Role of the S-S Bridge in Retroviral Protease Function and Virion Maturation
skos:notation
RIV/60461373:22330/07:00019201!RIV08-AV0-22330___
n3:strany
1493-1504
n3:aktivita
n4:Z n4:P
n3:aktivity
P(1M0520), P(IAA4055304), Z(MSM6046137305)
n3:cisloPeriodika
365
n3:dodaniDat
n9:2008
n3:domaciTvurceVysledku
n5:9372040
n3:druhVysledku
n18:J
n3:duvernostUdaju
n7:S
n3:entitaPredkladatele
n19:predkladatel
n3:idSjednocenehoVysledku
448239
n3:idVysledku
RIV/60461373:22330/07:00019201
n3:jazykVysledku
n14:eng
n3:klicovaSlova
retroviral protease; Mason-Pfizer monkey virus; disulfide; dimerization; maturation
n3:klicoveSlovo
n6:retroviral%20protease n6:maturation n6:dimerization n6:Mason-Pfizer%20monkey%20virus n6:disulfide
n3:kodStatuVydavatele
BE - Belgické království
n3:kontrolniKodProRIV
[296DF7D2B5E0]
n3:nazevZdroje
Journal of molecular biology
n3:obor
n17:EE
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
7
n3:projekt
n11:1M0520 n11:IAA4055304
n3:rokUplatneniVysledku
n9:2007
n3:tvurceVysledku
Hrabal, Richard Pichová, Iva Ruml, Tomáš Kluh, Ivan Tůma, Roman Svatoš, Aleš Zábranská, Helena
n3:zamer
n12:MSM6046137305
s:issn
0022-2836
s:numberOfPages
12
n16:organizacniJednotka
22330