Binding of ribosomal protein S1 of Escherichia coli to the 3' end of 16S rRNA.
- 1 August 1975
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 72 (8) , 2940-2944
- https://doi.org/10.1073/pnas.72.8.2940
Abstract
Ribosomal protein S1 reversibly binds the 49-nucleotide fragment that is cleaved from the 3' end of 16S rRNA in ribosomes by colicin E3. The fragment has secondary structure in the form of a hairpin loop. At the base of the stem is a sequence (A-C-C-U-C-C) thought to be involved in the base pairing with complementary sequences in mRNA during the initiation of protein synthesis. The role of S1 may be to stabilize this region of the fragment in an open conformation to allow for base pairing to mRNA. This model is supported by the observation that S1 binds specifically to this region of the fragment. In addition, aurin tricarboxylic acid, an inhibitor of protein synthesis, reverses this effect by disrupting the S1-RNA complex. These results can explain why S1 is an essential component of the ribosome for translation of natural mRNA and why aurin tricarboxylic acid blocks initiation.Keywords
This publication has 24 references indexed in Scilit:
- Two Forms of the 30 S Ribosomal Subunit of Escherichia coliJournal of Biological Chemistry, 1974
- Identification of protein S 1 at the messenger RNA binding site of the Escherichia coli ribosomeBiochemical and Biophysical Research Communications, 1974
- Interaction of Escherichia coli 30S Ribosomal Subunits with MS2 Phage RNA in the Absence of Initiation FactorsProceedings of the National Academy of Sciences, 1974
- Inhibition of synthetic and natural messenger translation. II. Specificity and mechanism of action of a protein isolated from Escherichia coli MRE 600 ribosomes.1974
- Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilusBiochemistry, 1974
- Structure and function of bacterial ribosomes. 24. Role of 16S ribosomal ribonucleic acid and the 30S ribosomal protein S12 in the initiation of natural messenger ribonucleic acid translationBiochemistry, 1974
- A protein-nucleic acid crosslink in 30s ribosomesBiochemical and Biophysical Research Communications, 1973
- Chemical modification of the transfer RNA and polyuridylic acid binding sites of Escherichia coli 30 s ribosomal subunitsJournal of Molecular Biology, 1971
- Specific Inactivation of 16S Ribosomal RNA Induced by Colicin E3 In VivoProceedings of the National Academy of Sciences, 1971
- Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gelsBiochemistry, 1968