Comparative nucleic acid chaperone properties of the nucleocapsid protein NCp7 and Tat protein of HIV-1

RNA chaperones are proteins able to rearrange nucleic acid structures towards their most stable conformations. In retroviruses, the reverse transcription of the viral RNA requires multiple and complex nucleic acid rearrangements that need to be chaperoned. HIV-1 has evolved different viral-encoded proteins with chaperone activity, notably Tat and the well described nucleocapsid protein NCp7. We propose here an overview of the recent reports that examine and compare the nucleic acid chaperone properties of Tat and NCp7 during reverse transcription to illustrate the variety of mechanisms of action of the nucleic acid chaperone proteins.

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► RNA chaperones are ubiquitous proteins that help to solve the folding problem.
► NCp7 and Tat are two HIV-1 encoded proteins with chaperone activity.
► We review the mode of action of Tat and NCp7 during reverse transcription.
► We illustrate the variety of mechanisms of action of RNA chaperone proteins.