at Google ScholarTitle data
Nowacka, Marzena ; Nowak, Elzbieta ; Czarnocki-Cieciura, Mariusz ; Jackiewicz, Justyna ; Skowronek, Krzysztof ; Szczepanowski, Roman H. ; Wöhrl, Birgitta M. ; Nowotny, Marcin:
Structures of substrate complexes of foamy viral protease-reverse transcriptase.
In: Journal of Virology.
Vol. 95
(2021)
Issue 18
.
- e00848-21.
ISSN 1098-5514
DOI: https://doi.org/10.1128/JVI.00848-21
Abstract in another language
Reverse transcriptases (RTs) use their DNA polymerase and RNase H activities to catalyze the conversion of single-stranded RNA to double-stranded DNA, a crucial process for the replication of retroviruses. Foamy viruses (FV) possess a unique RT which is a fusion with the protease (PR) domain. The mechanism of substrate binding by this enzyme has been unknown. Here, we report a crystal structure of monomeric full-length marmoset FV (MFV) PR-RT in complex with an RNA/DNA hybrid substrate. We also describe a structure of MFV PR-RT with RNase H deletion in complex with a dsDNA substrate in which the enzyme forms an asymmetric homodimer. Cryo-electron microscopy reconstruction of full-length MFV PR-RT - dsDNA complex confirmed the dimeric architecture. These findings represent the first structural description of nucleic acid binding by a foamy viral RT and demonstrate its ability to change its oligomeric state depending on the type of bound nucleic acid.