Primary structure of protein L23 from the Escherichia coli ribosome
نویسندگان
چکیده
منابع مشابه
Crystal structure of the ribosome recycling factor from Escherichia coli.
We have determined the crystal structure of the Escherichia coli ribosome recycling factor (RRF), which catalyzes the disassembly of the termination complex in protein synthesis. The L-shaped molecule consists of two domains: a triple-stranded antiparallel coiled-coil and an alpha/beta domain. The coil domain has a cylindrical shape and negatively charged surface, which are reminiscent of the a...
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The assembly of the Escherichia coli ribosome is based on many specific interactions between the ribosomal components. Direct evidence for single proteinRNA interactions has been well established (reviewed in ref. [l] ). Various observations provide circumstantial support for the existence of protein-protein complexes in the ribosome. For example, cooperative protein binding effects have been o...
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Bromoacetyl-phenylalanyl-tRNA(phe) bound to 70S E. coli ribosomes reacts covalently with proteins of the 50S subunit. The major reactions are with proteins L2 and L27. In the presence of poly(U), 70S-bound bromoacetyl-phenylalanyl-tRNA(phe) can participate in peptidebond formation with phenylalanyl-tRNA(phe) or puromycin. Most of the products of these reactions are also found covalently attache...
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Ribosomes were isolated from E. coli, strain P, as previously described [S] . After extraction of ribosomal proteins by acetic acid protein S6 was separated from the other proteins by a two step elution procedure followed by a gradient elution on DEAE-cellulose. This resulted in several forms of S6 as described below and elsewhere in detail [4]. Amino acid analyses were done on a Durrum D-500 a...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1979
ISSN: 0014-5793
DOI: 10.1016/0014-5793(79)81181-3