Reconstitution of Active 30-S Ribosomal Subunits in vitro Using Heat-Denatured 16-S rRNA
نویسندگان
چکیده
منابع مشابه
Reconstitution of functionally active Thermus aquaticus large ribosomal subunits with in vitro-transcribed rRNA.
Functionally active large ribosomal subunits of thermophilic bacterium Thermus aquaticus have been assembled in vitro from ribosomal proteins and either natural or in vitro-transcribed 23S rRNA and 5S rRNA. Sedimentation properties of reconstituted subunits were similar to those of native ribosomal 50S subunits. Subunits reconstituted with in vitro-transcribed rRNAs exhibited high activity in t...
متن کاملMapping ribosomal protein S20-16 S rRNA interactions by mutagenesis.
Specific ribonucleotides within the 5' domain of Escherichia coli 16 S rRNA were altered by deletion and/or substitution by site-directed mutagenesis of cloned DNA to assess the importance of these particular residues in defining the binding site for ribosomal protein S20. Gel filtration and sucrose gradient centrifugation were employed to measure the binding of ribosomal protein S20 to synthet...
متن کاملX - Ray Crystal Structure of a Ribosomal Protein S 6 , S 15 , S 18 : rRNA Complex from T . thermophilus , and Investigation of Conformational Changes in 16 S rRNA
.............................................................. 2 Chapter 1: A Golden Age of Ribosome Structural Biology ....................................................... 5 1.1 The ribosome is central to all living organisms ................... 5 1.2 30S particles can assemble independently ....................... 9 1.3 30S central domain an interesting target for detailed structural inves...
متن کاملBinding of 16 S rRNA to
Protein-RNA associations were studied by a method using proteins blotted on a nitrocellulose sheet. This method was assayed with Escherichia Coli 30S ribosomal components. In stringent conditions (300 mM NaCl or 20" C) only 9 E. coli ribosomal proteins strongly bound to the 16S rRNA: S4, S5, S7, S9, S127~ST3^~S14, S19, S20. 8 of these proteins have been previously found to bind independently to...
متن کاملRibosomal components from Escherichia coli 50 S subunits involved in the reconstitution of peptidyltransferase activity.
Incubation of 50 S subunits from Escherichia coli in the presence of 1.5 M LiCl yielded 1 . 5 ~ core particles which contained -20 proteins and were inactive with respect to peptidyltransferase activity. The proteins of the split fraction were isolated and their effects with respect to restoration of activity were tested in reconstitution assays. Purified L16 was able to restore activity, but t...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb13217.x