Structure of a beheaded 30 S ribosomal subunit from Thermus thermophilus.
The 22 S ribonucleoproten particles containing the 5' (body) and the central (platform) domains of the Thermus thermophilus 30 S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16 S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30 S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30 S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30 S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30 S subunit is a requisite for their correct fitting.
Serdyuk
I
I
Institute of Protein Research, Pushchino, Moscow Region, 142292, Russia. serdyuk@vega.protres.ru
Ulitin
A
A
Kolesnikov
I
I
Vasiliev
V
V
Aksenov
V
V
Zaccai
G
G
Svergun
D
D
Kozin
M
M
Willumeit
R
R
D003198:Computer Simulation; D008854:Microscopy, Electron; D009502:Neutrons; D016914:Ribonuclease H; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000648:ultrastructure; D012270:Ribosomes / Q000737:chemistry*; D012542:Scattering, Radiation; D016963:Thermus thermophilus / Q000737:chemistry*; D014461:Ultracentrifugation
D012261:Ribonucleoproteins; D016914:Ribonuclease H