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Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies.

1995; Springer Nature; Volume: 14; Issue: 18 Linguagem: Inglês

10.1002/j.1460-2075.1995.tb00137.x

1460-2075

Henning Urlaub, Volker Kruft, Oliver F. Bischof, Eva Müller, Brigitte Wittmann‐Liebold,

Peptidase Inhibition and Analysis

Research Article15 September 1995free access Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. H. Urlaub H. Urlaub Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author V. Kruft V. Kruft Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author O. Bischof O. Bischof Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author E. C. Müller E. C. Müller Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author B. Wittmann-Liebold B. Wittmann-Liebold Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author H. Urlaub H. Urlaub Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author V. Kruft V. Kruft Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author O. Bischof O. Bischof Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author E. C. Müller E. C. Müller Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author B. Wittmann-Liebold B. Wittmann-Liebold Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. Search for more papers by this author Author Information H. Urlaub1, V. Kruft1, O. Bischof1, E. C. Müller1 and B. Wittmann-Liebold1 1Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany. The EMBO Journal (1995)14:4578-4588https://doi.org/10.1002/j.1460-2075.1995.tb00137.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We have investigated protein-rRNA cross-links formed in 30S and 50S ribosomal subunits of Escherichia coli and Bacillus stearothermophilus at the molecular level using UV and 2-iminothiolane as cross-linking agents. We identified amino acids cross-linked to rRNA for 13 ribosomal proteins from these organisms, namely derived from S3, S4, S7, S14, S17, L2, L4, L6, L14, L27, L28, L29 and L36. Several other peptide stretches cross-linked to rRNA have been sequenced in which no direct cross-linked amino acid could be detected. The cross-linked amino acids are positioned within loop domains carrying RNA binding features such as conserved basic and aromatic residues. One of the cross-linked peptides in ribosomal protein S3 shows a common primary sequence motif–the KH motif–directly involved in interaction with rRNA, and the cross-linked amino acid in ribosomal protein L36 lies within the zinc finger-like motif of this protein. The cross-linked amino acids in ribosomal proteins S17 and L6 prove the proposed RNA interacting site derived from three-dimensional models. A comparison of our structural data with mutations in ribosomal proteins that lead to antibiotic resistance, and with those from protein-antibiotic cross-linking experiments, reveals functional implications for ribosomal proteins that interact with rRNA. Previous ArticleNext Article Volume 14Issue 181 September 1995In this issue RelatedDetailsLoading ...