Abstract
The DNA-directed synthesis of beta-galactosidase in Escherichia coli extracts has been investigated in a partially fractionated system. A dependency was obtained for 3',5'-cyclic AMP receptor protein and also for a factor, from the salt wash of ribosomes, that has been purified to near homogeneity. This factor has been identified with a ribosome release factor previously purified from the supernatant fraction by A. Hirashima and A. Kaji [(1972) Biochemistry 11,4037-4044]. In the coupled transcription-translation system this factor stimulates beta-galactosidase synthesis and total protein synthesis 2- to 4-fold. It is thus clear that the ribosome release factor has a physiological function in translation. It may also affect transcription, because it stimulated total RNA synthesis up to 50% in this in vitro system.
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- Capecchi M. R., Klein H. A. Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harb Symp Quant Biol. 1969;34:469–477. doi: 10.1101/sqb.1969.034.01.053. [DOI] [PubMed] [Google Scholar]
- Crepin M., Cukier-Kahn R., Gros F. Effect of a low-molecular-weight DNA binding protein, H1 factor, on the in vitro transcription of the lactose operon in Escherichia coli. Proc Natl Acad Sci U S A. 1975 Jan;72(1):333–337. doi: 10.1073/pnas.72.1.333. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cukier-Kahn R., Jacquet M., Gros F. Two heat-resistant, low molecular weight proteins from Escherichia coli that stimulate DNA-directed RNA synthesis. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3643–3647. doi: 10.1073/pnas.69.12.3643. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Davison J., Pilarski L. M., Echols H. A factor that stimulates RNA synthesis by purified RNA polymerase. Proc Natl Acad Sci U S A. 1969 May;63(1):168–174. doi: 10.1073/pnas.63.1.168. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hirashima A., Kaji A. Purification and properties of ribosome-releasing factor. Biochemistry. 1972 Oct 24;11(22):4037–4044. doi: 10.1021/bi00772a005. [DOI] [PubMed] [Google Scholar]
- Kung H. F., Brot N., Spears C., Chen B., Weissbach H. Studies on the in vitro transcription and translation of the lac operon. Arch Biochem Biophys. 1974 Jan;160(1):168–174. doi: 10.1016/s0003-9861(74)80023-8. [DOI] [PubMed] [Google Scholar]
- Kung H. F., Fox J. E., Spears C., Brot N., Weissbach H. Studies on the role of ribosomal proteins L 7 and L 12 in the in vitro synthesis of -galactosidase. J Biol Chem. 1973 Jul 25;248(14):5012–5015. [PubMed] [Google Scholar]
- Kung H. F., Morrissey J., Revel M., Spears C., Weissbach H. Studies on the lactose operon. The control of DNA-directed in vitro protein synthesis by interference factor i-alpha. J Biol Chem. 1975 Nov 25;250(22):8780–8784. [PubMed] [Google Scholar]
- Kung H. F., Spears C., Schulz T., Weissbach H. Studies on the in vitro synthesis of beta-galactosidase: necessary components in the ribosomal wash. Arch Biochem Biophys. 1974 Jun;162(2):578–584. doi: 10.1016/0003-9861(74)90218-5. [DOI] [PubMed] [Google Scholar]
- Kung H. F., Spears C., Weissbach H. DNA-directed in vitro synthesis of beta-galactosidase: dependencies on elongation factor Tu and tRNA. Arch Biochem Biophys. 1976 May;174(1):100–104. doi: 10.1016/0003-9861(76)90328-3. [DOI] [PubMed] [Google Scholar]
- Kung H., Spears C., Weissbach H. Purification and properties of a soluble factor required for the deoxyribonucleic acid-directed in vitro synthesis of beta-galactosidase. J Biol Chem. 1975 Feb 25;250(4):1556–1562. [PubMed] [Google Scholar]
- LEBOY P. S., COX E. C., FLAKS J. G. THE CHROMOSOMAL SITE SPECIFYING A RIBOSOMAL PROTEIN IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1964 Dec;52:1367–1374. doi: 10.1073/pnas.52.6.1367. [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]
- Leavitt J. C., Moldave K., Nakada D. Stimulation of in vitro RNA synthesis by ribosomes and ribosomal proteins. J Mol Biol. 1972 Sep 14;70(1):15–40. doi: 10.1016/0022-2836(72)90161-1. [DOI] [PubMed] [Google Scholar]
- Lee-Huang S., Ochoa S. Purification and properties of two messenger-discriminating species of E. coli initiation factor 3. Arch Biochem Biophys. 1973 May;156(1):84–96. doi: 10.1016/0003-9861(73)90344-5. [DOI] [PubMed] [Google Scholar]
- Lee-Huang S., Sillero M. A., Ochoa S. Isolation and properties of crystalline initiation factor F1 from Escherichia coli ribosomes. Eur J Biochem. 1971 Feb;18(4):536–543. doi: 10.1111/j.1432-1033.1971.tb01274.x. [DOI] [PubMed] [Google Scholar]
- Mahadik S. P., Srinivasan P. R. Stimulation of DNA-dependent RNA synthesis by a protein associated with ribosomes. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1898–1901. doi: 10.1073/pnas.68.8.1898. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murooka Y., Lazzarini R. A. Stimulation of RNA synthesis by two protein factors in extracts of Escherichia coli. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2336–2340. doi: 10.1073/pnas.69.8.2336. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nakamura H., Pisano J. J. Sensitive fluorometric assay for proteins: use of fluorescamine and membrane filters. Arch Biochem Biophys. 1976 Jan;172(1):102–105. doi: 10.1016/0003-9861(76)90052-7. [DOI] [PubMed] [Google Scholar]
- Ogawa K., Kaji A. Requirement for ribosome-releasing factor for the release of ribosomes at the termination codon. Eur J Biochem. 1975 Oct 15;58(2):411–419. doi: 10.1111/j.1432-1033.1975.tb02388.x. [DOI] [PubMed] [Google Scholar]
- Palacios R., Palmiter R. D., Schimke R. T. Identification and isolation of ovalbumin-synthesizing polysomes. I. Specific binding of 125 I-anti-ovalbumin to polysomes. J Biol Chem. 1972 Apr 25;247(8):2316–2321. [PubMed] [Google Scholar]
- Remold-O'Donnell E., Thach R. E. A new method for the purification of initiation factor F2 in high yield, and an estimation of stoichiometry in the binding reaction. J Biol Chem. 1970 Nov 10;245(21):5737–5742. [PubMed] [Google Scholar]
- Rouvière-Yaniv J., Gros F. Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3428–3432. doi: 10.1073/pnas.72.9.3428. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Subramanian A. R., Davis B. D. Release of 70 S ribosomes from polysomes in Escherichia coli. J Mol Biol. 1973 Feb 15;74(1):45–56. doi: 10.1016/0022-2836(73)90353-7. [DOI] [PubMed] [Google Scholar]
- Tai P. C., Wallace B. J., Herzog E. L., Davis B. D. Properties of initiation-free polysomes of Escherichia coli. Biochemistry. 1973 Feb;12(4):609–615. doi: 10.1021/bi00728a007. [DOI] [PubMed] [Google Scholar]
- Tate W. P., Beaudet A. L., Caskey C. T. Influence of guanine nucleotides and elongation factors on interaction of release factors with the ribosome. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2350–2355. doi: 10.1073/pnas.70.8.2350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tompkins R. K., Scolnick E. M., Caskey C. T. Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release. Proc Natl Acad Sci U S A. 1970 Mar;65(3):702–708. doi: 10.1073/pnas.65.3.702. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Travers A. A., Kamen R. I., Schleif R. F. Factor necessary for ribosomal RNA synthesis. Nature. 1970 Nov 21;228(5273):748–751. doi: 10.1038/228748a0. [DOI] [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]
- Zubay G., Lederman M. DNA-directed peptide synthesis. VI. Regulating the expression of the lac operon in a cell-free system. Proc Natl Acad Sci U S A. 1969 Feb;62(2):550–557. doi: 10.1073/pnas.62.2.550. [DOI] [PMC free article] [PubMed] [Google Scholar]