TY - JOUR
T1 - Architecture of the Pontin/Reptin Complex, Essential in the Assembly of Several Macromolecular Complexes
AU - Torreira, Eva
AU - Jha, Sudhakar
AU - López-Blanco, José R.
AU - Arias-Palomo, Ernesto
AU - Chacón, Pablo
AU - Cañas, Cristina
AU - Ayora, Sylvia
AU - Dutta, Anindya
AU - Llorca, Oscar
N1 - Funding Information:
This work was supported by projects SAF2005-00775 and SAF2008-00451 (O.L.), BFU2006-02907 (S.A.), and BFU2007-65977/BMC (P.C.) from the Spanish Ministry of Science, CAM S-BIO-0214-2006 (O.L. and P.C.) from the Autonomous Region of Madrid and CA89406 from the National Institutes of Health (A.D.). Llorca's group was additionally supported by project RD06/0020/1001 of the Red Temática Investigación Cooperativa en Cáncer (RTICC) and the Human Frontiers Science Program Organization (RGP39/2008). E.A.P. was supported by a contract from the Autonomous Region of Madrid. We are very thankful for help provided by Jaime Martin-Benito, Gabriel Piedrafita, Javier Varela, Emilia Aporta, and Dolores Alonso. We are also grateful for the support of the computing resources from the Galicia Supercomputer Centre (CESGA) and the Barcelona Supercomputing Centre, Spain.
PY - 2008/10/8
Y1 - 2008/10/8
N2 - Pontin 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.
AB - Pontin 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.
KW - CELLBIO
KW - PROTEINS
UR - http://www.scopus.com/inward/record.url?scp=53049099436&partnerID=8YFLogxK
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U2 - 10.1016/j.str.2008.08.009
DO - 10.1016/j.str.2008.08.009
M3 - Article
C2 - 18940606
AN - SCOPUS:53049099436
SN - 0969-2126
VL - 16
SP - 1511
EP - 1520
JO - Structure
JF - Structure
IS - 10
ER -