Literature DB >> 9693099

Precise determination of RNA-protein contact sites in the 50 S ribosomal subunit of Escherichia coli.

B Thiede1, H Urlaub, H Neubauer, G Grelle, B Wittmann-Liebold.   

Abstract

RNA-protein cross-linked complexes were isolated and purified to obtain precise data about RNA-protein contact sites in the 50 S ribosomal subunit of Escherichia coli. N-terminal microsequencing and matrix-assisted laser desorption ionization MS were used to identify the cross-linking sites at the amino acid and nucleotide levels. In this manner the following contact sites of five ribosomal proteins with the 23 S rRNA were established: Lys-67 of L2 to U-1963, Tyr-35 of L4 to U-615, Lys-97 of L21 to U-546, Lys-49 of L23 to U-139 or C-140 and Lys-71 and Lys-74 of L27 to U-2334.

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Year:  1998        PMID: 9693099      PMCID: PMC1219658          DOI: 10.1042/bj3340039

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  33 in total

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Journal:  Nucleic Acids Res       Date:  1990-12-11       Impact factor: 16.971

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Review 4.  The structure of ribosomal RNA: a three-dimensional jigsaw puzzle.

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Review 5.  RNA recognition: a family matter?

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Review 6.  Conserved structures and diversity of functions of RNA-binding proteins.

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Authors:  A A Beauclerk; E Cundliffe
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10.  Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies.

Authors:  H Urlaub; V Kruft; O Bischof; E C Müller; B Wittmann-Liebold
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  10 in total

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