Protein synthesis at atomic resolution: mechanistics of translation in the light of highly resolved structures for the ribosome. 2002

Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestr. 73, Berlin, D-14195 Berlin, Germany.

Our understanding of the process of translation has progressed rapidly since the availability of highly resolved structures for the ribosome. A wealth of information has emerged in terms of both RNA and protein structure and the interplay between them. This has prompted us to revisit the astonishing "treasure trove" of functional data regarding the ribosome that has accumulated over the past decades. Here we try a systematic synopsis of these ribosomal functions in light of the cryo-electron microscopic structures (resolution >7 A) and the atomic x-ray structures (>2.4 A) of the ribosome.

UI MeSH Term Description Entries
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
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
D010444 Peptide Elongation Factor Tu A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP. Elongation Factor Tu,EF-Tu,Eucaryotic Elongation Factor Tu,Protein Synthesis Elongation Factor Tu,eEF-Tu,EF Tu,Factor Tu, Elongation,eEF Tu
D010448 Peptide Initiation Factors Protein factors uniquely required during the initiation phase of protein synthesis in GENETIC TRANSLATION. Initiation Factors,Initiation Factor,Factors, Peptide Initiation,Initiation Factors, Peptide
D010452 Peptide Biosynthesis The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules. Biosynthesis, Peptide
D010454 Peptide Termination Factors Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors. Termination Release Factor,Factor, Termination Release,Factors, Peptide Termination,Release Factor, Termination,Termination Factors, Peptide
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
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D012269 Ribosomal Proteins Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits. Proteins, Ribosomal,Ribosomal Protein,Protein, Ribosomal
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

Related Publications

Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
January 2003, Methods in enzymology,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
December 2009, Cell,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
March 2001, Biochemistry,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
October 2000, Structure (London, England : 1993),
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
July 2014, Proceedings of the National Academy of Sciences of the United States of America,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
April 2001, Current opinion in structural biology,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
October 2000, Nature structural biology,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
August 2001, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
December 2020, International journal of biological macromolecules,
Daniel N Wilson, and Gregor Blaha, and Sean R Connell, and Pavel V Ivanov, and Holger Jenke, and Ulrich Stelzl, and Yoshika Teraoka, and Knud H Nierhaus
November 2005, Science (New York, N.Y.),
Copied contents to your clipboard!