mRNA containing an extended Shine-Dalgarno sequence is translated independently of ribosomal protein S1.
The role of ribosomal protein S1 in the translation of mRNA containing an extended Shine-Dalgarno sequence was investigated. Using the toeprinting technique, formation of the ternary initiation complex between 30S subunits, both S1-depleted or treated with anti-S1 antibodies, and mini-mRNA containing the 9 nucleotide-long Shine-Dalgarno sequence was studied. It was concluded that the initiation of translation on mRNA with an extended Shine-Dalgarno sequence is S1-independent. It was demonstrated that S1-depleted ribosomes effectively translate the cro-mini-mRNA in a cell-free system. In contrast to cro-mini-mRNA, 30S subunits without protein S1 are inactive in ternary initiation complex formation with, and cell-free translation of, MS2 or fr phage RNAs and RNA protein III of phage fd.
Balakin
A G
AG
Moscow State University, Russia.
Bogdanova
S L
SL
Skripkin
E A
EA
D001483:Base Sequence; D004247:DNA; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D012317:RNA Phages / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000737:chemistry / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics
D012333:RNA, Messenger; D012269:Ribosomal Proteins; D014764:Viral Proteins; C015494:ribosomal protein S1; D004247:DNA