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Exchange of functional domains between a bacterial conjugative relaxase and the integrase of the human adeno-associated virus

Abstract:

Endonucleases of the HUH family are specialized in processing single-stranded DNA in a variety of evolutionarily highly conserved biological processes related to mobile genetic elements. They share a structurally defined catalytic domain for site-specific nicking and strand-transfer reactions, which is often linked to the activities of additional functional domains, contributing to their overall versatility. To assess if these HUH domains could be interchanged, we created a chimeric protein f...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1371/journal.pone.0200841

Authors


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Role:
Author
ORCID:
0000-0001-7014-6804
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Role:
Author
ORCID:
0000-0002-7691-0735
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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Jenner Institute
Department:
Oxford,MSD,Jenner Institute
Role:
Author
ORCID:
0000-0002-1611-7655
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Role:
Author
ORCID:
0000-0002-4826-2240
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Grant:
grant1001764toRML
MR/N022890/1toEH
Publisher:
Public Library of Science Publisher's website
Journal:
PLoS ONE Journal website
Volume:
13
Issue:
7
Article number:
e0200841
Publication date:
2018-07-17
Acceptance date:
2018-07-02
DOI:
ISSN:
1932-6203
Pmid:
30016371
Source identifiers:
891219
Language:
English
Pubs id:
pubs:891219
UUID:
uuid:800e5e71-81e4-4a34-ad2a-2fb508c870db
Local pid:
pubs:891219
Deposit date:
2018-08-30

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