Conserved nucleotides of 23 S rRNA located at the ribosomal peptidyltransferase center. 1996

C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany. nierhaus_kh@mpimg-berlin-dahlem.mpg.de

Two nucleotides of the 23 S rRNA gene were mutated; the nucleotides correspond to the first two positions of the universally conserved sequence PsiGG2582 at the peptidyltransferase ring of 23 S rRNA. The ribosomes containing the altered 23 S rRNA were analyzed. Previously, it was shown that ribosomal assembly was indistinguishable from that in wild-type cells, that the flow of the corresponding 50 S subunit into the polysome fraction was not restricted, but that the ribosomes were strongly impaired in poly(Phe) synthesis (C. M. T. Spahn, J. Remme, M. A. Schäfer, and K. H. Nierhaus (1996) J. Biol. Chem. 271, 32849-32856). Here we apply assay systems exclusively testing the puromycin reaction of ribosomes carrying plasmid-born rRNA, a dipeptide assay using the minimal P site donor pA(fMet) and a translocation system not depending on the puromycin reaction. The mutations in helix 90 exclusively abolish or severely impair the ribosome capability to catalyze AcPhe-puromycin formation. A possible explanation of these observations is that G2581 and Psi2580 (and possibly also G2582) are part of the binding site of C75 of peptidyl-tRNA in the P site. The results suggest that in this case, however, such an interaction would disobey canonical base pairing.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009690 Nucleic Acid Conformation The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape. DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D010458 Peptidyl Transferases Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases. Peptidyl Transferase,Peptidyl Translocase,Peptidyl Translocases,Peptidyltransferase,Transpeptidase,Transpeptidases,Peptidyltransferases,Transferase, Peptidyl,Transferases, Peptidyl,Translocase, Peptidyl,Translocases, Peptidyl
D011691 Puromycin A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis. CL-13900,P-638,Puromycin Dihydrochloride,Puromycin Hydrochloride,Stylomycin,CL 13900,CL13900,P 638,P638
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D012338 RNA, Ribosomal, 23S Constituent of 50S subunit of prokaryotic ribosomes containing about 3200 nucleotides. 23S rRNA is involved in the initiation of polypeptide synthesis. 23S Ribosomal RNA,23S rRNA,RNA, 23S Ribosomal,Ribosomal RNA, 23S,rRNA, 23S
D012360 RNA, Transfer, Phe A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis. Phenylalanine-Specific tRNA,Transfer RNA, Phe,tRNAPhe,tRNA(Phe),Phe Transfer RNA,Phenylalanine Specific tRNA,RNA, Phe Transfer,tRNA, Phenylalanine-Specific

Related Publications

C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
February 1998, Biochemistry,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
July 1977, European journal of biochemistry,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
February 1997, Journal of molecular biology,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
January 2001, Journal of molecular biology,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
April 2000, Journal of molecular biology,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
October 1991, Journal of molecular biology,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
March 1999, FEBS letters,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
June 1994, The Journal of biological chemistry,
C M Spahn, and M A Schäfer, and A A Krayevsky, and K H Nierhaus
April 1970, FEBS letters,
Copied contents to your clipboard!