Functional study of the residue C899 in the 900 tetraloop of Escherichia coli small subunit ribosomal RNA.
A mutant ribosome bearing C899G in the 900 tetraloop of Escherichia coli 16S rRNA, one implicated in a conformational switch in the dynamic movements of the ribosome, showed defects in subunit association and 30S initiation complex formation. Our results explain the basis of the loss of protein synthesis ability caused by a perturbation of the 900 tetraloop.
Ha
Hye-Jeong
HJ
Department of Life Science, Chung-Ang University, Seoul, Republic of Korea.
Song
Woo-Seok
WS
Kim
Hong-Man
HM
Son
Ho-Sun
HS
Lee
Kangseok
K
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016296:Mutagenesis; D009690:Nucleic Acid Conformation; D010442:Peptide Chain Initiation, Translational; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D054679:Ribosome Subunits, Small / Q000235:genetics* / Q000378:metabolism
D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D012336:RNA, Ribosomal, 16S