Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A

Dovega, Rebecca; Tsutakawa, Susan; Quistgaard, Esben M.; Anandapadamanaban, Madhanagopal; Löw, Christian; Nordlund, Pär

doi:10.1371/journal.pone.0101846

Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A

Journal Article · Wed Jul 09 00:00:00 EDT 2014 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0101846· OSTI ID:1627717

Dovega, Rebecca ^[1]; Tsutakawa, Susan ^[2]; Quistgaard, Esben M. ^[3]; Anandapadamanaban, Madhanagopal ^[4]; Löw, Christian ^[3]; Nordlund, Pär ^[5]

Karolinska Institutet, Stockholm (Sweden). Dept. of Medical Biochemistry and Biophysics; DOE/OSTI
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Karolinska Institutet, Stockholm (Sweden). Dept. of Medical Biochemistry and Biophysics
Karolinska Institutet, Stockholm (Sweden). Dept. of Medical Biochemistry and Biophysics; Linkoping Univ. (Sweden). Dept. of Physics, Chemistry and Biology
Karolinska Institutet, Stockholm (Sweden). Dept. of Medical Biochemistry and Biophysics; Nanyang Technological Univ. (Singapore). School of Biological Sciences

Protein Phosphatase 2A (PP2A) is a major Ser/Thr phosphatase involved in the regulation of various cellular processes. PP2A assembles into diverse trimeric holoenzymes, which consist of a scaffolding (A) subunit, a catalytic (C) subunit and various regulatory (B) subunits. Here we report a 2.0 A crystal structure of the free B’’/PR70 subunit and a SAXS model of an A/PR70 complex. The crystal structure of B’’/PR70 reveals a two domain elongated structure with two Ca²⁺ binding EF-hands. Furthermore, we have characterized the interaction of both binding partner and their calcium dependency using biophysical techniques. Ca²⁺ biophysical studies with Circular Dichroism showed that the two EF-hands display different affinities to Ca2+. In the absence of the catalytic C-subunit, the scaffolding A-subunit remains highly mobile and flexible even in the presence of the B’’/PR70 subunit as judged by SAXS. Isothermal Titration Calorimetry studies and SAXS data support that PR70 and the A-subunit have high affinity to each other. This study provides additional knowledge about the structural basis for the function of B’’ containing holoenzymes.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: Danish Council for Independent Research; USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1627717

Journal Information:: PLoS ONE, Journal Name: PLoS ONE Journal Issue: 7 Vol. 9; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
Crystal structure
built structures
gel filtration
glycerol
isothermal titration calorimetry
molecular dynamics
phosphatases
small-angle scattering

Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A

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