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Topography of the E site on the Escherichia coli ribosome.

1993; Springer Nature; Volume: 12; Issue: 2 Linguagem: Inglês

10.1002/j.1460-2075.1993.tb05694.x

1460-2075

Jacek Wower, P Scheffer, Lee A. Sylvers, Wolfgang Wintermeyer, Robert A. Zimmermann,

Bacteriophages and microbial interactions

Research Article1 February 1993free access Topography of the E site on the Escherichia coli ribosome. J. Wower J. Wower Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author P. Scheffer P. Scheffer Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author L.A. Sylvers L.A. Sylvers Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author W. Wintermeyer W. Wintermeyer Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author R.A. Zimmermann R.A. Zimmermann Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author J. Wower J. Wower Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author P. Scheffer P. Scheffer Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author L.A. Sylvers L.A. Sylvers Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author W. Wintermeyer W. Wintermeyer Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author R.A. Zimmermann R.A. Zimmermann Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. Search for more papers by this author Author Information J. Wower1, P. Scheffer1, L.A. Sylvers1, W. Wintermeyer1 and R.A. Zimmermann1 1Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003. The EMBO Journal (1993)12:617-623https://doi.org/10.1002/j.1460-2075.1993.tb05694.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Three photoreactive tRNA probes have been utilized in order to identify ribosomal components that are in contact with the aminoacyl acceptor end and the anticodon loop of tRNA bound to the E site of Escherichia coli ribosomes. Two of the probes were derivatives of E. coli tRNA(Phe) in which adenosines at positions 73 and 76 were replaced by 2-azidoadenosine. The third probe was derived from yeast tRNA(Phe) by substituting wyosine at position 37 with 2-azidoadenosine. Despite the modifications, all of the photoreactive tRNA species were able to bind to the E site of E. coli ribosomes programmed with poly(A) and, upon irradiation, formed covalent adducts with the ribosomal subunits. The tRNA(Phe) probes modified at or near the 3′ terminus exclusively labeled protein L33 in the 50S subunit. The tRNA(Phe) derivative containing 2-azidoadenosine within the anticodon loop became cross-linked to protein S11 as well as to a segment of the 16S rRNA encompassing the 3′-terminal 30 nucleotides. We have located the two extremities of the E site-bound tRNA on the ribosomal subunits according to the positions of L33, S11 and the 3′ end of 16S rRNA defined by immune electron microscopy. Our results demonstrate conclusively that the E site is topographically distinct from either the P site or the A site, and that it is located alongside the P site as expected for the tRNA exit site. Previous ArticleNext Article Volume 12Issue 21 February 1993In this issue RelatedDetailsLoading ...