Mass spectrometry of hydrogen/deuterium exchange in 70S ribosomal proteins from E. coli.
The 70S ribosome from Escherichia coli is a supermacro complex (MW: 2.7MDa) comprising three RNA molecules and more than 50 proteins. We have for the first time successfully analyzed the flexibility of 70S ribosomal proteins in solution by detecting the hydrogen/deuterium exchange with mass spectrometry. Based on the deuterium incorporation map of the X-ray structure obtained at the time of each exchange, we demonstrate the structure-flexibility-function relationship of ribosome focusing on the deuterium incorporation of the proteins binding ligands (tRNA, mRNA, and elongation factor) and the relation with structural assembly processes.
Yamamoto
Tatsuya
T
Center for Quantum Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan. tyamamot@hiroshima-u.ac.jp
Izumi
Shunsuke
S
Gekko
Kunihiko
K
D041961:Deuterium Exchange Measurement; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D012269:Ribosomal Proteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D012269:Ribosomal Proteins