A robust method to quantitatively visualize HIV-1 replication complexes in infected cells shows that these complexes remain associated with the viral capsid beyond nuclear import in primary macrophages.
Cryo-EM structure and biochemical characterization of the human nuclear exosome reveals its specific properties with respect to the yeast complex, underscoring the evolutionary conservation of the RNA-channeling mechanisms and hMTR4 helicase recruitment.
Interaction of HIV capsids with the cellular protein cleavage-and-polyadenylation factor 6 at the inner side of nuclear pores promotes nuclear entry of the viral replication complex in primary human macrophages.
Cryo-EM structures of the 30S*RNAP complex visualize co-localization of the transcription and translation machineries and provide insights into the transcription-translation synchrony, which coordinates gene expression in bacteria.
Conformational flexibility in HIV-1 capsid, provided by cyclophilin A binding, facilitates evasion of capsid-targeting restriction factor MxB, while allowing sequence change to facilitate cytotoxic T-cell evasion.