Biophysical studies of the nucleic acid chaperone properties of the HIV-1 nucleocapsid protein.
The nucleocapsid protein NCp7 of HIV-1 possesses nucleic acid chaperone properties that are thought to be crucial throughout the viral life cycle. These properties promote the rearrangement of nucleic acids into their most thermodynamically stable conformations. These NCp7 properties involve two components, namely nucleic acid destabilization and activation of the annealing of complementary sequences. Biophysical techniques have been found extremely powerful to decipher the molecular mechanisms underlying these two components. We propose here an overview of the recent reports that examine the nucleic acid chaperone properties of NCp7 by these techniques.
Laboratoire de Biophotonique et Pharmacologie, Université de Strasbourg, Illkirch, France.
Julien
J
Godet
Yves
Y
Mély
D015497:HIV-1 / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D009696:Nucleic Acids / Q000378:metabolism; D054301:gag Gene Products, Human Immunodeficiency Virus / Q000737:chemistry / Q000378:metabolism*
D018832:Molecular Chaperones; C071884:NCP7 protein, Human immunodeficiency virus 1; D009696:Nucleic Acids; D054301:gag Gene Products, Human Immunodeficiency Virus