A Temperature-dependent Conformational Rearrangement in the Ribosomal Protein S4 ˙16 S rRNA Complex
نویسندگان
چکیده
منابع مشابه
X - 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...
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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...
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Digestion of reconstituted complexes of 16 S RNA and ribosomal protein S4 with pancreatic ribonuclease, followed by resolution of the products on polyacrylamide gels of low ionic strength, gives rise to a protected ribonucleoprotein fragment with a mobility of 7 S. Fingerprinting of the RNA moiety indicates the presence of sequences covering the 5' one-third of the 16 S RNA. After its extractio...
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Localized hydroxyl radical probing has been used to explore the rRNA neighborhood around a unique position in the structure of the Escherichia coli 30S ribosomal subunit. Fe(II) was attached to ribosomal protein S4 at Cys-31 via the reagent 1-(p-bromoacetamidobenzyl)-EDTA. [FeCys31]S4 was then complexed with 16S rRNA or incorporated into active 30S ribosomal subunits by in vitro reconstitution ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.3.1238