Release factor binding to ribosome requires an intact 16 S rRNA 3' terminus.
نویسندگان
چکیده
منابع مشابه
Binding 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 کاملInvolvement of helix 34 of 16 S rRNA in decoding and translocation on the ribosome.
Helix 34 of 16 S rRNA is located in the head of the 30 S ribosomal subunit close to the decoding center and has been invoked in a number of ribosome functions. In the present work, we have studied the effects of mutations in helix 34 both in vivo and in vitro. Several nucleotides in helix 34 that are either highly conserved or form important tertiary contacts in 16 S rRNA (U961, C1109, A1191, a...
متن کاملEffect of mutations in the A site of 16 S rRNA on aminoglycoside antibiotic-ribosome interaction.
Decoding of genetic information occurs upon interaction of an mRNA codon-tRNA anticodon complex with the small subunit of the ribosome. The ribosomal decoding region is associated with highly conserved sequences near the 3' end of 16 S rRNA. The decoding process is perturbed by the aminoglycoside antibiotics, which also interact with this region of rRNA. Mutations of certain nucleotides in rRNA...
متن کاملFast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3.
A complete translation system has been assembled from pure initiation, elongation and termination factors as well as pure aminoacyl-tRNA synthetases. In this system, ribosomes perform repeated rounds of translation of short synthetic mRNAs which allows the time per translational round (the recycling time) to be measured. The system has been used to study the influence of release factor RF3 and ...
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P2X7 receptors (P2X7Rs) are ATP-gated ion channels that display the unusual property of current facilitation during long applications of agonists. Here we show that facilitation disappears in chimeric P2X7Rs containing the C-terminus of the P2X2 receptor (P2X2R), and in a truncated P2X7R missing the cysteine-rich domain of the C-terminus. The chimeric and truncated receptors also show an appare...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40178-5