Document Detail

Structural requirements for enzymatic activities of foamy virus protease-reverse transcriptase.
MedLine Citation:
PMID:  23966123     Owner:  NLM     Status:  Publisher    
Reverse transcriptases (RTs) are pivotal in the life cycle of retroviruses and convert the genomic viral RNA into double stranded DNA. The RT polymerase domain is sub-divided into fingers, palm, thumb and the connection subdomain, which links the polymerase to the C-terminal RNase H domain. In contrast to orthoretroviruses, mature RT of foamy viruses harbors the protease (PR) domain at its N-terminus (PR-RT). Therefore and due to low homology to other RTs, it is difficult to define the boundaries and functions of the (sub)domains. We introduced N- and C-terminal deletions into simian foamy virus PR-RT to investigate the impact of the truncations on the catalytic activities. Both, the RNase H domain and the connection subdomain contribute substantially to polymerase integrity and stability as well as to polymerase activity and substrate binding. The 42 amino acids long region C-terminal of the PR is important for polymerase stability and activity. PR activation via binding of PR-RT to viral RNA requires the presence of the full length PR-RT including the RNase H domain. In vitro, the cleavage efficiencies of FV PR for the Gag and Pol cleavage site are comparable, even though in virus particles only the Pol site is cleaved to completion suggesting that additional factors control PR activity and that virus maturation needs to be strictly regulated. © Proteins 2013;. © 2013 Wiley Periodicals, Inc.
Anna Schneider; Daniel Peter; Jessica Schmitt; Berit Leo; Franziska Richter; Paul Rösch; Birgitta M Wöhrl; Maximilian J Hartl
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-8-22
Journal Detail:
Title:  Proteins     Volume:  -     ISSN:  1097-0134     ISO Abbreviation:  Proteins     Publication Date:  2013 Aug 
Date Detail:
Created Date:  2013-8-22     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Wiley Periodicals, Inc., a Wiley company.
Universität Bayreuth, Lehrstuhl Biopolymere, Universitätsstr. 30, D-95447, Bayreuth, Germany.
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