Literature DB >> 10496220

Orientation of the tRNA anticodon in the ribosomal P-site: quantitative footprinting with U33-modified, anticodon stem and loop domains.

S S Ashraf1, R Guenther, P F Agris.   

Abstract

Binding of transfer RNA (tRNA) to the ribosome involves crucial tRNA-ribosomal RNA (rRNA) interactions. To better understand these interactions, U33-substituted yeast tRNA(Phe) anticodon stem and loop domains (ASLs) were used as probes of anticodon orientation on the ribosome. Orientation of the anticodon in the ribosomal P-site was assessed with a quantitative chemical footprinting method in which protection constants (Kp) quantify protection afforded to individual 16S rRNA P-site nucleosides by tRNA or synthetic ASLs. Chemical footprints of native yeast tRNA(Phe), ASL-U33, as well as ASLs containing 3-methyluridine, cytidine, or deoxyuridine at position 33 (ASL-m3U33, ASL-C33, and ASL-dU33, respectively) were compared. Yeast tRNAPhe and the ASL-U33 protected individual 16S rRNA P-site nucleosides differentially. Ribosomal binding of yeast tRNA(Phe) enhanced protection of C1400, but the ASL-U33 and U33-substituted ASLs did not. Two residues, G926 and G1338 with KpS approximately 50-60 nM, were afforded significantly greater protection by both yeast tRNA(Phe) and the ASL-U33 than other residues, such as A532, A794, C795, and A1339 (KpS approximately 100-200 nM). In contrast, protections of G926 and G1338 were greatly and differentially reduced in quantitative footprints of U33-substituted ASLs as compared with that of the ASL-U33. ASL-m3U33 and ASL-C33 protected G530, A532, A794, C795, and A1339 as well as the ASL-U33. However, protection of G926 and G1338 (KpS between 70 and 340 nM) was significantly reduced in comparison to that of the ASL-U33 (43 and 61 nM, respectively). Though protections of all P-site nucleosides by ASL-dU33 were reduced as compared to that of the ASL-U33, a proportionally greater reduction of G926 and G1338 protections was observed (KpS = 242 and 347 nM, respectively). Thus, G926 and G1338 are important to efficient P-site binding of tRNA. More importantly, when tRNA is bound in the ribosomal P-site, G926 and G1338 of 16S rRNA and the invariant U33 of tRNA are positioned close to each other.

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Year:  1999        PMID: 10496220      PMCID: PMC1369842          DOI: 10.1017/s1355838299990933

Source DB:  PubMed          Journal:  RNA        ISSN: 1355-8382            Impact factor:   4.942


  24 in total

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Journal:  Nucleic Acids Res       Date:  1989-11-11       Impact factor: 16.971

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Authors:  H F Noller; V Hoffarth; L Zimniak
Journal:  Science       Date:  1992-06-05       Impact factor: 47.728

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Authors:  D Moazed; H F Noller
Journal:  J Mol Biol       Date:  1990-01-05       Impact factor: 5.469

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Authors:  U von Ahsen; H F Noller
Journal:  Science       Date:  1995-01-13       Impact factor: 47.728

5.  "Footprint" titrations yield valid thermodynamic isotherms.

Authors:  M Brenowitz; D F Senear; M A Shea; G K Ackers
Journal:  Proc Natl Acad Sci U S A       Date:  1986-11       Impact factor: 11.205

6.  The time dependence of chemical modification reveals slow steps in the folding of a group I ribozyme.

Authors:  A R Banerjee; D H Turner
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Review 7.  tRNA-rRNA interactions and peptidyl transferase.

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9.  Hydroxyl radical cleavage of tRNA in the ribosomal P site.

Authors:  A Hüttenhofer; H F Noller
Journal:  Proc Natl Acad Sci U S A       Date:  1992-09-01       Impact factor: 11.205

10.  The decoding region of 16S RNA; a cross-linking study of the ribosomal A, P and E sites using tRNA derivatized at position 32 in the anticodon loop.

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Journal:  EMBO J       Date:  1994-06-01       Impact factor: 11.598

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Review 4.  Diverse Mechanisms of Sulfur Decoration in Bacterial tRNA and Their Cellular Functions.

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Review 5.  Extracurricular Functions of tRNA Modifications in Microorganisms.

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