Linked Life Data

10517582

Source:http://linkedlifedata.com/resource/pubmed/id/10517582

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-1-10
pubmed:databankReference
pubmed:abstractText
The tsf genes from Streptomyces coelicolor A3(2) and Streptomyces ramocissimus, encoding the guanine-nucleotide exchange factor EF-Ts, were cloned and sequenced. Streptomycetes have multiple and highly divergent EF-Tu species, with EF-Tu1 and EF-Tu3 showing only about 65% amino acid sequence identity, and yet these can apparently interact with a single EF-Ts species. tsf lies in an operon with rpsB, which encodes ribosomal protein S2. The amino acid sequence of S2 from S. coelicolor differs from most other bacterial S2 homologues in having a C-terminal extension of 70 aa residues with a highly repetitive organization, the function of which is unknown. Transcription analysis of the rpsB-tsf operon of S. coelicolor by promoter probing, nuclease S1 mapping and Northern blotting revealed that the genes give rise to a bicistronic transcript from a single promoter upstream of rpsB. An attenuator was identified in the rpsB-tsf intergenic region; it results in an approximately 2:1 ratio of rpsB vs tsf transcripts. Although tuf1, encoding the major EF-Tu, is located in the rpsL ribosomal protein operon, an additional promoter in the fus-tuf1 intergenic region leads to a significant excess of EF-Tu over ribosomes. Most amino acid residues known from the Escherichia coli crystal structure of the EF-Tu-EF-Ts complex to be directly involved in interaction between the two elongation factors are conserved between E. coli and Streptomyces. However, whenever interaction residues in the EF-Tu moiety show divergence among Streptomyces EF-Tu1, EF-Tu2 and EF-Tu3, the single Streptomyces EF-Ts exhibits compensatory substitutions of the corresponding residues. These apparently enable productive interaction to occur with all three EF-Tus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
145 ( Pt 9)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2293-301
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10517582-Amino Acid Sequence, pubmed-meshheading:10517582-Base Sequence, pubmed-meshheading:10517582-Blotting, Southern, pubmed-meshheading:10517582-Cloning, Molecular, pubmed-meshheading:10517582-Gene Expression Regulation, Bacterial, pubmed-meshheading:10517582-Molecular Sequence Data, pubmed-meshheading:10517582-Multigene Family, pubmed-meshheading:10517582-Operon, pubmed-meshheading:10517582-Peptide Elongation Factor Tu, pubmed-meshheading:10517582-Peptide Elongation Factors, pubmed-meshheading:10517582-Promoter Regions, Genetic, pubmed-meshheading:10517582-Restriction Mapping, pubmed-meshheading:10517582-Ribosomal Proteins, pubmed-meshheading:10517582-Sequence Analysis, DNA, pubmed-meshheading:10517582-Streptomyces, pubmed-meshheading:10517582-Transcription, Genetic
pubmed:year
1999
pubmed:articleTitle
Evidence that a single EF-Ts suffices for the recycling of multiple and divergent EF-Tu species in Streptomyces coelicolor A3(2) and Streptomyces ramocissimus.
pubmed:affiliation
Department of Biochemistry, Leiden Institute of Chemistry, Leiden University, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't