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Título

Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes

Autor Torreira, Eva ; Jha, Sudhakar; López-Blanco, José R.; Arias-Palomo, Ernesto ; Chacón, Pablo ; Cañas, Cristina; Ayora, Silvia; Dutta, Anindya; Llorca, Óscar
Palabras clave Proteins
Cellular Biology
Fecha de publicación 7-oct-2008
EditorElsevier
Citación Structure 16(10): 1511-1520 (2008)
ResumenPontin and reptin belong to the AAA+ family, and they are essential for the structural integrity and catalytic activity of several chromatin remodeling complexes. They are also indispensable for the assembly of several ribonucleoprotein complexes, including telomerase. Here, we propose a structural model of the yeast pontin/reptin complex based on a cryo-electron microscopy reconstruction at 13 Å. Pontin/reptin hetero-dodecamers were purified from in vivo assembled complexes forming a double ring. Two rings interact through flexible domains projecting from each hexamer, constituting an atypical asymmetric form of oligomerization. These flexible domains and the AAA+ cores reveal significant conformational changes when compared with the crystal structure of human pontin that generate enlarged channels. This structure of endogenously assembled pontin/reptin complexes is different than previously described structures, suggesting that pontin and reptin could acquire distinct structural states to regulate their broad functions as molecular motors and scaffolds for nucleic acids and proteins.
Descripción 10 pages, 6 figures.-- PMID: 18940606 [PubMed].-- PMCID: PMC2577609 [Available on 2009/10/01].-- Supplementary information (Suppl. figures S1-S5, 5 pages) available at: http://www.structure.org/cgi/content/full/16/10/1511/DC1/
The cryo-EM map of yeast pontin/reptin complex has been deposited in the 3D EM database (http://www.ebi.ac.uk/msd/) under accession code EMD-2865.
Versión del editorhttp://dx.doi.org/10.1016/j.str.2008.08.009
URI http://hdl.handle.net/10261/9456
DOI10.1016/j.str.2008.08.009
ISSN0969-2126
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