Location of 5.8 S rRNA contact sites in 28 S rRNA and the effect of alpha-sarcin on the association of 5.8 S rRNA with 28 S rRNA.
نویسندگان
چکیده
منابع مشابه
Pactamycin resistance mutations in functional sites of 16 S rRNA.
Mutants of an archaeon Halobacterium halobium, resistant to the universal inhibitor of translation, pactamycin, were isolated. Pactamycin resistance correlated with the presence of mutations in the 16 S rRNA gene of H. halobium single rRNA operon. Three types of mutations were found in pactamycin resistant cells, A694G, C795U and C796U (Escherichia coli 16 S rRNA numeration) located distantly i...
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 کامل5 S rRNA: structure and interactions.
5 S rRNA is an integral component of the large ribosomal subunit in all known organisms. Despite many years of intensive study, the function of 5 S rRNA in the ribosome remains unknown. Advances in the analysis of ribosome structure that have revealed the crystal structures of large ribosomal subunits and of the complete ribosome from various organisms put the results of studies on 5 S rRNA in ...
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 کاملMutations in domain II of 23 S rRNA facilitate translation of a 23 S rRNA-encoded pentapeptide conferring erythromycin resistance.
Mutations in domain II of Escherichia coli 23 S rRNA that cause resistance to erythromycin do so in a manner fundamentally different from mutations at the drug binding site in domain V of the 23 S rRNA. The domain II mutations are located in a hairpin structure between nucleotides 1198 and 1247. This is close to a short open reading frame in the 23 S rRNA that encodes a pentapeptide (E-peptide)...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)33261-7