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Structures of substrate complexes of foamy viral protease-reverse transcriptase

Title 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 (July 2021) .
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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Chair Biopolymers - Apl. Prof. Dr. Birgitta Wöhrl
Research Institutions > Research Centres > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 09 Jul 2021 08:38
Last Modified: 09 Jul 2021 08:38
URI: https://eref.uni-bayreuth.de/id/eprint/66516