@article{Maertens:2016:nar/gkv1347,
author = {Maertens, GNE},
doi = {nar/gkv1347},
journal = {Nucleic Acids Research},
pages = {364--376},
title = {B'-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase},
url = {http://dx.doi.org/10.1093/nar/gkv1347},
volume = {44},
year = {2016}
}

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TY  - JOUR
AB  - To establish infection, a retrovirus must insert a DNA copy of its RNA genome into host chromatin. This reaction is catalysed by the virally encoded enzyme integrase (IN) and is facilitated by viral genus-specific host factors. Herein, cellular serine/threonine protein phosphatase 2A (PP2A) is identified as a functional IN binding partner exclusive to δ-retroviruses, including human T cell lymphotropic virus type 1 and 2 (HTLV-1 and HTLV-2) and bovine leukaemia virus (BLV). PP2A is a heterotrimer composed of a scaffold, catalytic and one of any of four families of regulatory subunits, and the interaction is specific to the B′ family of the regulatory subunits. B′-PP2A and HTLV-1 IN display nuclear co-localization, and the B′ subunit stimulates concerted strand transfer activity of δ-retroviral INs in vitro. The protein–protein interaction interface maps to a patch of highly conserved residues on B′, which when mutated render B′ incapable of binding to and stimulating HTLV-1 and -2 IN strand transfer activity.
AU  - Maertens,GNE
DO  - nar/gkv1347
EP  - 376
PY  - 2016///
SN  - 1362-4962
SP  - 364
TI  - B'-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase
T2  - Nucleic Acids Research
UR  - http://dx.doi.org/10.1093/nar/gkv1347
UR  - http://hdl.handle.net/10044/1/27828
VL  - 44
ER  - 

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