In order to evaluate the effect of cationic copolymer structures on their nucleic acid-chaperoning activity, we prepared various copolymers having different cationic residues or backbone molecular weight. It was revealed that nucleic acid-chaperoning activity increases with increasing molecular weight of the copolymer backbone and that the copolymer having the guanidino groups is effective for increasing nucleic acid-chaperoning activity. Compared with PLL-g-Dex, GPLL-g-Dex has weak activity to stabilize ds DNA. This weak stabilization effect of GPLL-g-Dex may contribute to the higher accelerating effect.
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http://dx.doi.org/10.1093/nass/nrl014 | DOI Listing |
PLoS One
June 2013
UMR5236 CNRS, UM1,UM2, CPBS, Montpellier, France.
Retroviral nucleocapsid proteins harbor nucleic acid chaperoning activities that mostly rely on the N-terminal basic residues and the CCHC zinc finger motif. Such chaperoning is essential for virus replication, notably for genomic RNA selection and packaging in virions, and for reverse transcription of genomic RNA into DNA. Recent data revealed that HIV-1 nucleocapsid restricts reverse transcription during virus assembly--a process called late reverse transcription--suggesting a regulation between RNA packaging and late reverse transcription.
View Article and Find Full Text PDFNucleic Acids Res
October 2011
Unité de Virologie Humaine INSERM, ENS, IFR 128, 46 allée d'Italie, 69364 Lyon, France.
Prion diseases are unique neurodegenerative illnesses associated with the conversion of the cellular prion protein (PrP(C)) into the aggregated misfolded scrapie isoform, named PrP(Sc). Recent studies on the physiological role of PrP(C) revealed that this protein has probably multiple functions, notably in cell-cell adhesion and signal transduction, and in assisting nucleic acid folding. In fact, in vitro findings indicated that the human PrP (huPrP) possesses nucleic acid binding and annealing activities, similarly to nucleic acid chaperone proteins that play essential roles in cellular DNA and RNA metabolism.
View Article and Find Full Text PDFRetroviral nucleocapsid (NC) is central to viral replication. Nucleic acid chaperoning is a key function for NC through the action of its conserved basic amino acids and zinc-finger structures. NC manipulates genomic RNA from its packaging in the producer cell to reverse transcription into the infected host cell.
View Article and Find Full Text PDFBiochemistry
November 2008
Institut Gilbert Laustriat, Photophysique des interactions moleculaires, UMR 7175 CNRS, Faculte de Pharmacie, Universite Louis Pasteur, Strasbourg 1, 74, Route du Rhin, 67401 Illkirch, France.
Conversion of the genomic RNA of human immunodeficiency virus (HIV) into full-length viral DNA is a complex multistep reaction catalyzed by the reverse transcriptase (RT). Numerous studies have shown that the viral nucleocapsid (NC) protein has a vital impact on various steps during reverse transcription, which is crucial for virus infection. However, the exact molecular details are poorly defined.
View Article and Find Full Text PDFNucleic Acids Res
June 2008
LaboRetro INSERM #758, Ecole Normale Supérieure de Lyon, IFR 128 Biosciences Lyon-Gerland, 69364 Lyon Cedex 07, France.
The human immunodeficiency virus type 1 (HIV-1) is a primate lentivirus that causes the acquired immunodeficiency syndrome (AIDS). In addition to the virion structural proteins and enzyme precursors, that are Gag, Env and Pol, HIV-1 encodes several regulatory proteins, notably a small nuclear transcriptional activator named Tat. The Tat protein is absolutely required for virus replication since it controls proviral DNA transcription to generate the full-length viral mRNA.
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