Literature DB >> 1907372

Mutations in 16S rRNA that affect UGA (stop codon)-directed translation termination.

H U Göringer1, K A Hijazi, E J Murgola, A E Dahlberg.   

Abstract

Site-directed mutagenesis was performed on a sequence motif within the 3' major domain of Escherichia coli 16S rRNA shown previously to be important for peptide chain termination. Analysis of stop codon suppression by the various mutants showed an exclusive response to UGA stop signals, which was correlated directly with the continuity of one or the other of two tandem complementary UCA sequences (bases 1199-1204). Since no other structural features of the mutated ribosomes were hampered and the translation initiation and elongation events functioned properly, we propose that a direct interaction occurs between the UGA stop codon on the mRNA and the 16S rRNA UCA motif as one of the initial events of UGA-dependent peptide chain termination. These results provide evidence that base pairing between rRNA and mRNA plays a direct role in termination, as it has already been shown to do for initiation and elongation.

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Year:  1991        PMID: 1907372      PMCID: PMC52135          DOI: 10.1073/pnas.88.15.6603

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  41 in total

1.  Mutants with base changes at the 3'-end of the 16S RNA from Escherichia coli. Construction, expression and functional analysis.

Authors:  N Rottmann; B Kleuvers; J Atmadja; R Wagner
Journal:  Eur J Biochem       Date:  1988-10-15

2.  Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension.

Authors:  D Moazed; S Stern; H F Noller
Journal:  J Mol Biol       Date:  1986-02-05       Impact factor: 5.469

3.  Spectinomycin resistance at site 1192 in 16S ribosomal RNA of E. coli: an analysis of three mutants.

Authors:  P C Makosky; A E Dahlberg
Journal:  Biochimie       Date:  1987-08       Impact factor: 4.079

4.  Compilation of small ribosomal subunit RNA sequences.

Authors:  E Dams; L Hendriks; Y Van de Peer; J M Neefs; G Smits; I Vandenbempt; R De Wachter
Journal:  Nucleic Acids Res       Date:  1988       Impact factor: 16.971

5.  Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites.

Authors:  D Moazed; H F Noller
Journal:  Cell       Date:  1989-05-19       Impact factor: 41.582

6.  A single base change in the Shine-Dalgarno region of 16S rRNA of Escherichia coli affects translation of many proteins.

Authors:  W F Jacob; M Santer; A E Dahlberg
Journal:  Proc Natl Acad Sci U S A       Date:  1987-07       Impact factor: 11.205

7.  Probing the phosphates of the Escherichia coli ribosomal 16S RNA in its naked form, in the 30S subunit, and in the 70S ribosome.

Authors:  F Baudin; M Mougel; P Romby; F Eyermann; J P Ebel; B Ehresmann; C Ehresmann
Journal:  Biochemistry       Date:  1989-07-11       Impact factor: 3.162

8.  Mutagenesis at the mRNA decoding site in the 16S ribosomal RNA using the specialized ribosome system in Escherichia coli.

Authors:  A S Hui; D H Eaton; H A de Boer
Journal:  EMBO J       Date:  1988-12-20       Impact factor: 11.598

9.  Reading frame switch caused by base-pair formation between the 3' end of 16S rRNA and the mRNA during elongation of protein synthesis in Escherichia coli.

Authors:  R B Weiss; D M Dunn; A E Dahlberg; J F Atkins; R F Gesteland
Journal:  EMBO J       Date:  1988-05       Impact factor: 11.598

10.  The Escherichia coli 30S ribosomal subunit; an optimized three-dimensional fit between the ribosomal proteins and the 16S RNA.

Authors:  D Schüler; R Brimacombe
Journal:  EMBO J       Date:  1988-05       Impact factor: 11.598

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  10 in total

1.  Mutations in E.coli 16s rRNA that enhance and decrease the activity of a suppressor tRNA.

Authors:  C D Prescott; H C Kornau
Journal:  Nucleic Acids Res       Date:  1992-04-11       Impact factor: 16.971

2.  A ribosomal ambiguity mutation in the 530 loop of E. coli 16S rRNA.

Authors:  M O'Connor; H U Göringer; A E Dahlberg
Journal:  Nucleic Acids Res       Date:  1992-08-25       Impact factor: 16.971

3.  Crystal structure of the Thermus thermophilus 16 S rRNA methyltransferase RsmC in complex with cofactor and substrate guanosine.

Authors:  Hasan Demirci; Steven T Gregory; Albert E Dahlberg; Gerwald Jogl
Journal:  J Biol Chem       Date:  2008-07-30       Impact factor: 5.157

4.  Intermolecular mRNA-rRNA hybridization and the distribution of potential interaction regions in murine 18S rRNA.

Authors:  O V Matveeva; S A Shabalina
Journal:  Nucleic Acids Res       Date:  1993-02-25       Impact factor: 16.971

5.  Mutations at U2555, a tRNA-protected base in 23S rRNA, affect translational fidelity.

Authors:  M O'Connor; A E Dahlberg
Journal:  Proc Natl Acad Sci U S A       Date:  1993-10-01       Impact factor: 11.205

6.  Comparative characterization of release factor RF-3 genes of Escherichia coli, Salmonella typhimurium, and Dichelobacter nodosus.

Authors:  Y Kawazu; K Ito; K Matsumura; Y Nakamura
Journal:  J Bacteriol       Date:  1995-10       Impact factor: 3.490

7.  Saturation mutagenesis of a +1 programmed frameshift-inducing mRNA sequence derived from a yeast retrotransposon.

Authors:  Carla Guarraia; Laura Norris; Ana Raman; Philip J Farabaugh
Journal:  RNA       Date:  2007-09-19       Impact factor: 4.942

8.  Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli.

Authors:  O Mikuni; K Ito; J Moffat; K Matsumura; K McCaughan; T Nobukuni; W Tate; Y Nakamura
Journal:  Proc Natl Acad Sci U S A       Date:  1994-06-21       Impact factor: 11.205

9.  Two regions of the Escherichia coli 16S ribosomal RNA are important for decoding stop signals in polypeptide chain termination.

Authors:  C M Brown; K K McCaughan; W P Tate
Journal:  Nucleic Acids Res       Date:  1993-05-11       Impact factor: 16.971

10.  Modular Organization of Residue-Level Contacts Shapes the Selection Pressure on Individual Amino Acid Sites of Ribosomal Proteins.

Authors:  Saurav Mallik; Sudip Kundu
Journal:  Genome Biol Evol       Date:  2017-04-01       Impact factor: 3.416

  10 in total

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