Mapping proteins of the 50S subunit from Escherichia coli ribosomes.
Mapping of protein positions in the ribosomal subunits was first achieved for the 30S subunit by means of neutron scattering about 15 years ago. Since the 50S subunit is almost twice as large as the 30S subunit and consists of more proteins, it was difficult to apply classical contrast variation techniques for the localisation of the proteins. Polarisation dependent neutron scattering (spin-contrast variation) helped to overcome this restriction. Here a map of 14 proteins within the 50S subunit from Escherichia coli ribosomes is presented including the proteins L17 and L20 that are not present in archeal ribosomes. The results are compared with the recent crystallographic map of the 50S subunit from the archea Haloarcula marismortui.
Willumeit
R
R
GKSS Forschungszentrum Geesthacht GmbH, Institut für Werkstoffforschung, WFS, Germany. regine.willumeit@gkss.de
Diedrich
G
G
Forthmann
S
S
Beckmann
J
J
May
R P
RP
Stuhrmann
H B
HB
Nierhaus
K H
KH
D003461:Crystallography; D003903:Deuterium; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D009502:Neutrons; D011522:Protons; D012335:RNA, Ribosomal / Q000302:isolation & purification; D012269:Ribosomal Proteins / Q000032:analysis / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry*; D012542:Scattering, Radiation
D011522:Protons; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; C029609:ribosomal protein L18; C036298:ribosomal protein L24; C031127:ribosomal protein L25; D003903:Deuterium