Structure of a beheaded 30 S ribosomal subunit from Thermus thermophilus

Citation
I. Serdyuk et al., Structure of a beheaded 30 S ribosomal subunit from Thermus thermophilus, J MOL BIOL, 292(3), 1999, pp. 633-639
Citations number
26
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Molecular Biology & Genetics
Journal title
JOURNAL OF MOLECULAR BIOLOGY
ISSN journal
0022-2836 → ACNP
Volume
292
Issue
3
Year of publication
1999
Pages
633 - 639
Database
ISI
SICI code
0022-2836(19990924)292:3<633:SOAB3S>2.0.ZU;2-X
Abstract
The 22 S ribonucleoproten particles containing the 5' (body) and the centra l (platform) domains of the Thermus thermophilus 30 S subunit has been stud ied by sedimentation, neutron scattering and electron microscopy. The RNP p articles have been obtained by oligonucleotide-directed cleavage of 16 S RN A with ribonulease H in the region of the 900th nucleotide of the protein-d eficient derivatives of the 30 S subunits. It is shown that these RNP parti cles are very compact, though their form and dimensions differ slightly fro m those expected from the electron microscopy model of the 30 S subunit beh eaded by computer simulation. The particles are subdivided into two structu ral domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30 S subunit. Electron microscopy demons trates that the mutual arrangement of domains in the RNP particles is not s trictly fixed suggesting that interaction with the third domain of the 30 S subunit is a requisite for their correct fitting. (C) 1999 Academic Press.