Structural Mapping of Divergent Regions in the Type 1 Ryanodine Receptor Using Fluorescence Resonance Energy Transfer

被引:8
作者
Mahalingam, Mohana [1 ]
Girgenrath, Tanya [1 ]
Svensson, Bengt [2 ]
Thomas, David D. [2 ]
Cornea, Razvan L. [2 ]
Fessenden, James D. [1 ]
机构
[1] Brigham & Womens Hosp, Dept Anesthesia Perioperat & Pain Med, Boston, MA 02115 USA
[2] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA
关键词
CALCIUM-RELEASE CHANNEL; MUSCLE SARCOPLASMIC-RETICULUM; SKELETAL-MUSCLE; 3-DIMENSIONAL RECONSTRUCTION; CA2+ RELEASE; CRYOELECTRON MICROSCOPY; FK506-BINDING PROTEIN; TRANSMEMBRANE DOMAINS; MOLECULAR-CLONING; LOCALIZATION;
D O I
10.1016/j.str.2014.07.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ryanodine receptors (RyRs) release Ca2+ to initiate striated muscle contraction. Three highly divergent regions (DRs) in the RyR protein sequence (DR1, DR2, and DR3) may confer isoform-specific functional properties to the RyRs. We used cell-based fluorescence resonance energy transfer (FRET) measurements to localize these DRs to the cryoelectron microscopic (cryo-EM) map of the skeletal muscle RyR isoform (RyR1). FRET donors were targeted to RyR1 using five different FKBP12.6 variants labeled with Alexa Fluor 488. FRET was then measured to the FRET acceptors, Cy3NTA or Cy5NTA, targeted to decahistidine tags introduced within the DRs. DR2 and DR3 were localized to separate positions within the "clamp" region of the RyR1 cryo-EM map, which is presumed to interface with Ca(v)1.1. DR1 was localized to the "handle" region, near the regulatory calmodulin-binding site on the RyR. These localizations provide insights into the roles of DRs in RyR allosteric regulation during excitation contraction coupling.
引用
收藏
页码:1322 / 1332
页数:11
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