NDLI: Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus

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Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus

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Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chen, S. R. Sharma, M. R. Liu, Z. Li, P. Wagenknecht, T. Zhang, J.
Description	Author Affiliation: Liu Z ( Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, USA. liuz@wadsworth.org);
Abstract	Recombinant type 3 ryanodine receptor (RyR3) has been purified in quantities sufficient for structural characterization by cryoelectron microscopy and three-dimensional (3D) reconstruction. Two cDNAs were prepared and expressed in HEK293 cells, one encoding the wild-type RyR3 and the other encoding RyR3 containing glutathione S-transferase (GST) fused to its amino terminus (GST-RyR3). RyR3 was purified from detergent-solubilized transfected cells by affinity chromatography using 12.6-kDa FK506-binding protein in the form of a GST fusion as the affinity ligand. Purification of GST-RyR3 was achieved by affinity chromatography by using glutathione-Sepharose. Purified recombinant RyR3 and GST-RyR3 proteins exhibited high-affinity [(3)H]ryanodine binding that was sensitive to activation by Ca(2+) and caffeine and to inhibition by Mg(2+). 3D reconstructions of both recombinant RyR3 and GST-RyR3 appeared very similar to that of the native RyR3 purified from bovine diaphragm. Comparison of the 3D reconstructions of RyR3 and GST-RyR3 revealed that the GST domains and, hence, the amino termini of the RyR3 subunits are located in the 'clamp' structures that form the corners of the square-shaped cytoplasmic region of homotetrameric RyR3. This study describes the 3D reconstruction of a recombinant ryanodine receptor and it demonstrates the potential of this technology for characterizing functional and structural perturbations introduced by site-directed mutagenesis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Ryanodine Receptor Calcium Release Channel Ultrastructure Cell Line Cryoelectron Microscopy Glutathione Transferase Genetics Isolation & Purification Protein Conformation Recombinant Fusion Proteins Physiology Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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