Release of ribosomal proteins from Escherichia coli ribosomes with high concentrations of lithium chloride |
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Authors: | T Itoh E Otaka S Osawa |
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Affiliation: | 1. Environmental Engineering Department, Council of Scientific & Industrial Research (CSIR) Central Leather Research Institute (CLRI), Adyar, Chennai, 600 020, Tamil Nadu, India;2. Environmental Science Lab, Council of Scientific & Industrial Research (CSIR) Central Leather Research Institute (CLRI), Adyar, Chennai, 600 020, Tamil Nadu, India;3. Department of Chemistry, SRM Institute of Science and Technology, Kattankulathur, Tamil Nadu, 603 203, India;4. SRMIST, Deemed University, Ramapuram Campus, Chennai, 600089, Tamil Nadu, India;5. Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, Uttar Pradesh, India;1. Department of Biochemistry and Molecular Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan;2. Division of Molecular Science, Graduate School of Science and Technology, Gunma University, 1-5-1, Tenjin-cho, Kiryu-shi, Gunma 376-8515, Japan;3. Department of Biological Science, Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan;1. Department of Physiology, UT Southwestern Medical Center, Dallas, TX 75390, USA;2. Cancer Biology Program and Mechanisms of Disease and Translational Science Track, UT Southwestern Medical Center, Dallas, TX 75390, USA;3. CFFT Lab, Cystic Fibrosis Foundation, Lexington, MA 02421, USA;1. Jining Key Laboratory of Immunology, Jining Medical University, Jining, 272067, China;2. Department of Public Health, Jining Medical University, Jining, 272067, China;1. Institute of Molecular and Cell Biology, University of Tartu, Riia 23B, Tartu, 51010, Estonia;2. Department of Molecular and Cell Biology, California Institute of Quantitative Biosciences, University of California, Berkeley, CA, 94720, USA;3. Institute of Technology, University of Tartu, Nooruse 1, 50411, Tartu, Estonia;1. Department of Cell Biology, SUNY Downstate Health Sciences University, Brooklyn, NY, USA |
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Abstract: | The sequential release of ribosomal proteins from Escherichia coli ribosomes under the influence of concentrated LiCl solutions was studied. Treatment of 50 s or 30 s ribosomal subunits with various concentrations of LiCl containing 2.5 × 10−2m-Tris buffer (pH 7.8) and 10−1m-magnesium acetate or 5 × 10−3m-EDTA produced a series of protein-deficient particles having sedimentation coefficients of 40, 36, 28 and 25 s (from a 50 s subunit), and of 25, 23, 21, 19 and 16 s (from a 30 s subunit). The protein components of these particles have been analysed by carboxymethyl-cellulose column chromatography. It was shown that release of protein from ribosomes does not occur in a random fashion but follows a certain definite order. Furthermore, this release proceeds in more or less discrete steps as already pointed out by Lerman, Spirin, Gavrilova &; Golov (1966).Ribonucleoprotein particles having a single (or two) protein component are obtained by exposing the 30 or 50 s ribosome subunits to 3.5 m-LiCl in the absence of magnesium ions for 82 hours. |
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