Document Detail


Changes in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation analysis.
MedLine Citation:
PMID:  16773394     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Data from polyphenylalanine [poly(Phe)] synthesis determination in the presence and in the absence of erythromycin have been used in conjunction with Molecular Dynamics Simulation analysis, in order to localize the functional sites affected by mutations of Thermus thermophilus ribosomal protein L4 incorporated in Escherichia coli ribosomes. We observed that alterations in ribosome capability to synthesize poly(Phe) in the absence of erythromycin were mainly correlated to shifts of A2062 and C2612 of 23S rRNA, while in the presence of erythromycin they were correlated to shifts of A2060 and U2584 of 23S rRNA. Our results suggest a means of understanding the role of the extended loop of L4 ribosomal protein in ribosomal peptidyltransferase center.
Authors:
G Papadopoulos; S Grudinin; D L Kalpaxis; T Choli-Papadopoulou
Related Documents :
7818544 - Synthesis of non-translating or translating specialized ribosomes causes feedback regul...
8219074 - A rice (oryza sativa l.) cdna encodes a protein sequence homologous to the eukaryotic r...
7538324 - Methylation of the conserved a1518-a1519 in escherichia coli 16s ribosomal rna by the k...
10960474 - A covariant change of the two highly conserved bases in the gtpase-associated center of...
17416664 - The phosphotransferase system formed by ptsp, ptso, and ptsn proteins controls producti...
16689994 - Ontogenetic variations in the venom proteome of the amazonian snake bothrops atrox.
Publication Detail:
Type:  Journal Article     Date:  2006-06-14
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  35     ISSN:  0175-7571     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-09-29     Completed Date:  2007-04-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  675-83     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Biotechnology, University of Thessaly, Ploutonos 26, 41221, Larissa, Greece. papg@chem.auth.gr
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Anti-Bacterial Agents / pharmacology
Erythromycin / pharmacology
Escherichia coli / drug effects,  genetics,  metabolism*
Models, Molecular
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Peptides / metabolism*
Peptidyl Transferases / chemistry,  metabolism*
Protein Conformation
RNA, Bacterial / genetics
RNA, Ribosomal, 23S / genetics
Ribosomal Proteins / chemistry,  genetics*,  metabolism
Ribosomes / genetics,  metabolism*
Thermus thermophilus / metabolism*
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Peptides; 0/RNA, Bacterial; 0/RNA, Ribosomal, 23S; 0/Ribosomal Proteins; 0/ribosomal protein L4; 114-07-8/Erythromycin; 30394-07-1/polyphenylalanine; EC 2.3.2.12/Peptidyl Transferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Invasive meningococcal disease in children in Greece: comparison of serogroup A disease with disease...
Next Document:  Abundance and chromosomal distribution of six Drosophila buzzatii transposons: BuT1, BuT2, BuT3, BuT...