Abstract
Amino acid incorporation directed by poly(A), poly(U) or R17 RNA has been examined in S1-depleted protein synthesizing systems. We observe that the translation of either synthetic or natural messenger RNA is strictly dependent on the presence of chain initiation factor 3 and ribosomal protein S1. With poly(A) or poly(U) both IF-3 and S1 stimulate amino acid incorporation at least 25-fold, and with R17 RNA the stimulation is approximately 15-fold. More than one copy of S1 per ribosome decreases amino acid incorporation directed by poly(U) or R17 RNA. Initiation complex formation with R17 RNA is also stimulated optimally by the addition of one copy of S1 per ribosome. The function of IF-3 and S1 in protein synthesis is considered.
Full text
PDF












Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bear D. G., Ng R., Van Derveer D., Johnson N. P., Thomas G., Schleich T., Noller H. F. Alteration of polynucleotide secondary structure by ribosomal protein S1. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1824–1828. doi: 10.1073/pnas.73.6.1824. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carmichael G. G. Isolation of bacterial and phage proteins by homopolymer RNA-cellulose chromatography. J Biol Chem. 1975 Aug 10;250(15):6160–6167. [PubMed] [Google Scholar]
- Czernilofsky A. P., Kurland C. G., Stöffler G. 30S ribosomal proteins associated with the 3'-terminus of 16S RNA. FEBS Lett. 1975 Oct 15;58(1):281–284. doi: 10.1016/0014-5793(75)80279-1. [DOI] [PubMed] [Google Scholar]
- Dahlberg A. E., Dahlberg J. E. Binding of ribosomal protein S1 of Escherichia coli to the 3' end of 16S rRNA. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2940–2944. doi: 10.1073/pnas.72.8.2940. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dahlberg A. E. Two forms of the 30 S ribosomal subunit of Escherichia coli. J Biol Chem. 1974 Dec 10;249(23):7673–7678. [PubMed] [Google Scholar]
- Fedoroff N. V., Zinder N. D. Structure of the poly(G) polymerase component of the bacteriophage f2 replicase. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1838–1843. doi: 10.1073/pnas.68.8.1838. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fiser I., Margaritella P., Kuechler E. Photoaffinity reaction between polyuridylic acid and protein S1 on the Escherichia coli ribosome. FEBS Lett. 1975 Apr 1;52(2):281–283. doi: 10.1016/0014-5793(75)80825-8. [DOI] [PubMed] [Google Scholar]
- Goldberg M. L., Steitz J. A. Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus. Biochemistry. 1974 May 7;13(10):2123–2129. doi: 10.1021/bi00707a020. [DOI] [PubMed] [Google Scholar]
- Hawley D. A., Miller M. J., Slobin L. I., Wahba A. J. The mechanism of action of initiation factor 3 in protein synthesis. I. Studies on ribosomes crosslinked with dimethylsuberimidate. Biochem Biophys Res Commun. 1974 Nov 6;61(1):329–337. doi: 10.1016/0006-291x(74)90570-1. [DOI] [PubMed] [Google Scholar]
- Hawley D. A., Slobin L. I., Wahba A. J. The mechanism of action of initiation factor 3 in protein synthesis. II. Association of the 30S ribosomal protein S12 with IF-3. Biochem Biophys Res Commun. 1974 Nov 27;61(2):544–550. doi: 10.1016/0006-291x(74)90991-7. [DOI] [PubMed] [Google Scholar]
- Held W. A., Gette W. R., Nomura M. Role of 16S ribosomal ribonucleic acid and the 30S ribosomal protein S12 in the initiation of natural messenger ribonucleic acid translation. Biochemistry. 1974 May 7;13(10):2115–2122. doi: 10.1021/bi00707a019. [DOI] [PubMed] [Google Scholar]
- Hermoso J. M., Szer W. Replacement of ribosomal protein S1 by interference factor ialpha in ribosomal binding of phage Ms2 RNA. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4708–4712. doi: 10.1073/pnas.71.12.4708. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hille M. B., Miller M. J., Iwasaki K., Wahba A. J. Translation of the genetic message. VI. The role of ribosomal subunits in binding of formylmethionyl-tRNA and its reaction with puromycin. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1652–1654. doi: 10.1073/pnas.58.4.1652. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Inouye H., Pollack Y., Petre J. Physical and functional homology between ribosomal protein S1 and interference factor i. Eur J Biochem. 1974 Jun 1;45(1):109–117. doi: 10.1111/j.1432-1033.1974.tb03535.x. [DOI] [PubMed] [Google Scholar]
- Iwasaki K., Sabol S., Wahba A. J., Ochoa S. Translation of the genetic message. VII. Role of initiation factors in formation of the chain initiation complex with Escherichia coli ribosomes. Arch Biochem Biophys. 1968 May;125(2):542–547. doi: 10.1016/0003-9861(68)90612-7. [DOI] [PubMed] [Google Scholar]
- Jay G., Kaempfer R. Translational repression of a viral messenger RNA by a host protein. J Biol Chem. 1975 Aug 10;250(15):5749–5755. [PubMed] [Google Scholar]
- Kenner R. A. A protein-nucleic acid crosslink in 30S ribosomes. Biochem Biophys Res Commun. 1973 Apr 16;51(4):932–938. doi: 10.1016/0006-291x(73)90016-8. [DOI] [PubMed] [Google Scholar]
- Kolakofsky D., Dewey K. F., Hershey J. W., Thach R. E. Guanosine 5'-triphosphatase activity of initiation factor f2. Proc Natl Acad Sci U S A. 1968 Nov;61(3):1066–1070. doi: 10.1073/pnas.61.3.1066. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Miller M. J., Niveleau A., Wahba A. J. Inhibition of synthetic and natural messenger translation. I. Purification and properties of a protein isolated from Escherichia coli MRE 600 ribosomes. J Biol Chem. 1974 Jun 25;249(12):3803–3807. [PubMed] [Google Scholar]
- Miller M. J., Wahba A. J. Chain initiation factor 2. Purification and properties of two species from Escherichia coli MRE 600. J Biol Chem. 1973 Feb 10;248(3):1084–1090. [PubMed] [Google Scholar]
- Miller M. J., Wahba A. J. Inhibition of synthetic and natural messenger translation. II. Specificity and mechanism of action of a protein isolated from Escherichia coli MRE 600 ribosomes. J Biol Chem. 1974 Jun 25;249(12):3808–3813. [PubMed] [Google Scholar]
- Schiff N., Miller M. J., Wahba A. J. Purification and properties of chain initiation factor 3 from T4-infected and uninfected Escherichia coli MRE 600. Stimulation of translation of synthetic and natural messengers. J Biol Chem. 1974 Jun 25;249(12):3797–3802. [PubMed] [Google Scholar]
- Senear A. W., Steitz J. A. Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs. J Biol Chem. 1976 Apr 10;251(7):1902–1912. [PubMed] [Google Scholar]
- Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steitz J. A., Jakes K. How ribosomes select initiator regions in mRNA: base pair formation between the 3' terminus of 16S rRNA and the mRNA during initiation of protein synthesis in Escherichia coli. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4734–4738. doi: 10.1073/pnas.72.12.4734. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Szer W., Hermoso J. M., Boublik M. Destabilization of the secondary structure of RNA by ribosomal protein S1 from Escherichia coli. Biochem Biophys Res Commun. 1976 Jun 7;70(3):957–964. doi: 10.1016/0006-291x(76)90685-9. [DOI] [PubMed] [Google Scholar]
- Szer W., Hermoso J. M., Leffler S. Ribosomal protein S1 and polypeptide chain initiation in bacteria. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2325–2329. doi: 10.1073/pnas.72.6.2325. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Szer W., Leffler S. Interaction of Escherichia coli 30S ribosomal subunits with MS2 phage RNA in the absence of initiation factors. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3611–3615. doi: 10.1073/pnas.71.9.3611. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tal M., Aviram M., Kanarek A., Weiss A. Polyuridylic acid binding and translating by Escherichia coli ribosomes: stimulation by protein I, inhibition by aurintricarboxylic acid. Biochim Biophys Acta. 1972 Oct 27;281(3):381–392. doi: 10.1016/0005-2787(72)90452-2. [DOI] [PubMed] [Google Scholar]
- Van Dieijen G., Van Der Laken C. J., Van Knippenberg P. H., Van Duin J. Function of Escherichia coli ribosomal protein S1 in translation of natural and synthetic messenger RNA. J Mol Biol. 1975 Apr 15;93(3):351–366. doi: 10.1016/0022-2836(75)90282-x. [DOI] [PubMed] [Google Scholar]
- Van Duin J., Kurland C. G., Dondon J., Grunberg-Mangago M., Branlant C., Ebel J. P. New aspects of the IF3-ribosome interaction. FEBS Lett. 1976 Feb 15;62(2):111–114. doi: 10.1016/0014-5793(76)80030-0. [DOI] [PubMed] [Google Scholar]
- Wahba A. J., Miller M. J. Chain initiation factors from Escherichia coli. Methods Enzymol. 1974;30:3–18. doi: 10.1016/0076-6879(74)30003-1. [DOI] [PubMed] [Google Scholar]
- Wahba A. J., Miller M. J., Niveleau A., Landers T. A., Carmichael G. G., Weber K., Hawley D. A., Slobin L. I. Subunit I of G beta replicase and 30 S ribosomal protein S1 of Escherichia coli. Evidence for the identity of the two proteins. J Biol Chem. 1974 May 25;249(10):3314–3316. [PubMed] [Google Scholar]
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
- van Duin J., van Knippenberg P. H. Functional heterogeneity of the 30 S ribosomal subunit of Escherichia coli. 3. Requirement of protein S1 for translation. J Mol Biol. 1974 Mar 25;84(1):185–195. doi: 10.1016/0022-2836(74)90221-6. [DOI] [PubMed] [Google Scholar]

