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Artículo

The PKA regulatory subunit from yeast forms a homotetramer: Low-resolution structure of the N-terminal oligomerization domain

González Bardeci, Nicolás DiegoIcon ; Caramelo, Julio JavierIcon ; Blumenthal, Donald K.; Rinaldi, Jimena JulietaIcon ; Rossi, Silvia; Moreno, Silvia MargaritaIcon
Fecha de publicación: 12/2015
Editorial: Elsevier
Revista: Journal Of Structural Biology
ISSN: 1047-8477
e-ISSN: 1095-8657
Idioma: Inglés
Tipo de recurso: Artículo publicado

Resumen

The cAMP dependent protein kinase (PKA) is a key enzyme involved in many cellular processes in eukaryotes. In mammals, the regulatory (R) subunit localises the catalytic (C) subunit to specific subcellular sites through the interaction of its N-terminal homodimeric docking and dimerization (D/D) domain with specific scaffold proteins. The structure of the D/D domain has been extensively studied in mammals, but there is little information from non-mammalian species. In this work, we present the structural analysis of the D/D domain of Bcy1, the R subunit of PKA from Saccharomyces cerevisiae. Using chemical crosslinking experiments and static light scattering measurements we found that this R subunit forms a tetramer in solution, unlike its dimeric mammalian counterparts. We determined that the D/D domain is responsible for this unusual oligomeric state. Using biophysical techniques including size-exclusion chromatography, sucrose gradient sedimentation, small angle X-ray scattering (SAXS), and circular dichroism, we performed a detailed structural characterization of the tetrameric D/D domain of Bcy1. We used homology modelling in combination with computer-aided docking methods and ab initio SAXS modelling methods to develop structural models for the D/D domain tetramer. The models consist of two homodimers with a canonical D/D domain fold that generate a dimer of dimers with novel putative interaction surfaces. These findings indicate that the oligomerization states of PKA R subunits is more diverse than previously thought, and suggest that this might allow some forms of PKA to interact with a wide range of intracellular partners.
Palabras clave: Pka , Saccharomyces Cerevisiae , Bcy1 , Dd
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/23615
URL: http://www.sciencedirect.com/science/article/pii/S1047847715301088
DOI: http://dx.doi.org/10.1016/j.jsb.2015.12.001
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Articulos(IIBBA)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Citación
González Bardeci, Nicolás Diego; Caramelo, Julio Javier; Blumenthal, Donald K.; Rinaldi, Jimena Julieta; Rossi, Silvia; et al.; The PKA regulatory subunit from yeast forms a homotetramer: Low-resolution structure of the N-terminal oligomerization domain; Elsevier; Journal Of Structural Biology; 193; 2; 12-2015; 141-154
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