Photosensitized cross‐linking of IF‐3 to <i>Escherichia coli</i> 30 S subunits

Cooperman, Barry S.; Dondon, J.; Finelli, Jacqueline; Grunberg‐Manago, Marianne; Michelson, A.M.

doi:10.1016/0014-5793(77)80120-8

Cited by 27 publications

(10 citation statements)

References 15 publications

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“…Immuno-EM located the factor at the cleft of the 30S ribosomal subunit (220). The ribosomal proteins S7, S11, S12, S13, S18, S19, and S21 have been cross-linked to IF3 but are spread over a wide area of the 30S subunit (13,33,34,117). Helices 26 (central domain) and 45 (3Ј minor domain) of the 16S rRNA have been cross-linked to IF3 (47).…”

Section: Bacillus Subtilis Is the Only Organism That Does Not Belong mentioning

confidence: 99%

Initiation of Protein Synthesis in Bacteria

Laursen

Sørensen

Mortensen

et al. 2005

Microbiol Mol Biol Rev

540

506

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Valuable information on translation initiation is available from biochemical data and recently solved structures. We present a detailed description of current knowledge about the structure, function, and interactions of the individual components involved in bacterial translation initiation. The first section describes the ribosomal features relevant to the initiation process. Subsequent sections describe the structure, function, and interactions of the mRNA, the initiator tRNA, and the initiation factors IF1, IF2, and IF3. Finally, we provide an overview of mechanisms of regulation of the translation initiation event. Translation occurs on ribonucleoprotein complexes called ribosomes. The ribosome is composed of a large subunit and a small subunit that hold the activities of peptidyltransfer and decode the triplet code of the mRNA, respectively. Translation initiation is promoted by IF1, IF2, and IF3, which mediate base pairing of the initiator tRNA anticodon to the mRNA initiation codon located in the ribosomal P-site. The mechanism of translation initiation differs for canonical and leaderless mRNAs, since the latter is dependent on the relative level of the initiation factors. Regulation of translation occurs primarily in the initiation phase. Secondary structures at the mRNA ribosomal binding site (RBS) inhibit translation initiation. The accessibility of the RBS is regulated by temperature and binding of small metabolites, proteins, or antisense RNAs. The future challenge is to obtain atomic-resolution structures of complete initiation complexes in order to understand the mechanism of translation initiation in molecular detail

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Section: Bacillus Subtilis Is the Only Organism That Does Not Belong mentioning

confidence: 99%

Initiation of Protein Synthesis in Bacteria

Laursen

Sørensen

Mortensen

et al. 2005

Microbiol Mol Biol Rev

540

506

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“…The initiation factor IF3, involved in promoting dissociation of vacant 70S ribosomes and binding mRNA during initiation of translation (:220), has long been suspected of binding to 16S rRNA. Cross-linking of IF3 to 16S rRNA has been achieved by photolysis using near-UV irradiation (221). At least one site of cross-linking is reported to be in the 3'-terminal region ; removal of the 3'-terminal colicin fragment decreases the binding of IF3 to 30S subunits.…”

Section: Mrna Interactions and Initiationmentioning

confidence: 99%

Structure of Ribosomal Rna

Noller¹

1984

Annu. Rev. Biochem.

752

305

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Ribosomes are ribonucleoprotein particles that are responsible for trans lation of the genetic code. Unlike other cellular polymerases, ribosomes typically contain 50 to 60 percent RNA as an integral part of their structures. It is an intriguing problem to understand why this is so, and its elucidation is likely to be inseparable from an understanding of the structure, function, assembly, and evolution ofthese particles. This review is an attempt to summarize recent progress in our understanding of ribo somal RNA (rRNA) structure, and to point out some of the implica

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“…This situation reflects both the technological gap in the development of protein-protein vs. protein-RNA cross-linking procedures, as well as the greater difficulty inherent in the unequivocal identification of short stretches of a long polynucleotide, such as the 16S rRNA, as compared with the identification of ribosomal proteins, which can easily be achieved by electrophoretic and immunological techniques. As far as IF-3 is concerned, a cross-linking between the factor and the 16S rRNA has so far been obtained by a photosensitization procedure (Cooperman et al, 1977) and by use of 3OS ribosomal subunits containing bromouracil (Gualerzi and Pongs, unpublished observations). In neither case, however, has the RNA region engaged in the cross-linking been identified.…”

mentioning

confidence: 99%

Crosslinking of Escherichia coli initiation factor IF-3 to the RNA moiety of the 30S ribosomal subunits

Pon¹,

Brimacombe²,

Gualerzi³

1977

Biochemistry

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Escherichia coli initiation factor IF-3 labeled in vitro by either reductive alkylation or reaction with TV-ethylmaleimide can be cross-linked to the 16S rRNA of 30S ribosomal subunits by irradiation with ultraviolet light or reaction with formaldehyde, respectively. In both cases, the cross-linking to the 16S rRNA appears to be direct and not mediated via ribosomal proteins. When cross-linking to 16S and 23S rRNAs is compared at short irradiation times or under conditions which depress nonspecific IF-3 binding, the factor is cross-linked two to three times more efficiently to the 16S than to the 23S rRNA. When cross-linked complexes of 30S and radioactive IF-3 are isolated and subjected to limited hydrolysis with RNase Tl, the 30S ribosomes are split into two subparticles which can be electrophoretically resolved; the two particles each contain a characteristic set of proteins with one The topographical localization of the IF-3 binding site on the 30S ribosomal subunit has been attempted by different techniques. The picture emerging from these studies is that, when bound to the ribosome, IF-3 is localized in a region probably adjacent to the subunit interface (Gualerzi et al., 1973) neighboring, at least in part, the 3' end of the 16S rRNA (van Duin et al., 1975) as well as ribosomal proteins SI, S7, SI 1,

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Photosensitized cross‐linking of IF‐3 to Escherichia coli 30 S subunits

Cited by 27 publications

References 15 publications

Initiation of Protein Synthesis in Bacteria

Initiation of Protein Synthesis in Bacteria

Structure of Ribosomal Rna

Crosslinking of Escherichia coli initiation factor IF-3 to the RNA moiety of the 30S ribosomal subunits

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