Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-3-11
pubmed:abstractText
Selection of the proper start codon for the synthesis of a polypeptide by the Escherichia coli translation initiation apparatus involves several macromolecular components. These macromolecules interact in a specific and concerted manner to yield the translation initiation complex. This review focuses on recent data concerning the properties of the initiator tRNA and of enzymes and factors involved in the translation initiation process. The three initiation factors, as well as methionyl-tRNA synthetase and methionyl-tRNA(f)Met formyltransferase are described. In addition, the tRNA recognition properties of EF-Tu and peptidyl-tRNA hydrolase are considered. Finally, peptide deformylase and methionine aminopeptidase, which catalyze the amino terminal maturation of nascent polypeptides, can also be associated to the translation initiation process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Anticodon, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Methionine-tRNA Ligase, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors, http://linkedlifedata.com/resource/pubmed/chemical/Prokaryotic Initiation Factor-2, http://linkedlifedata.com/resource/pubmed/chemical/Prokaryotic Initiation Factor-3, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Met, http://linkedlifedata.com/resource/pubmed/chemical/aminoacyl-tRNA hydrolase, http://linkedlifedata.com/resource/pubmed/chemical/methionyl aminopeptidase, http://linkedlifedata.com/resource/pubmed/chemical/peptide deformylase
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
543-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8955898-Amidohydrolases, pubmed-meshheading:8955898-Aminopeptidases, pubmed-meshheading:8955898-Anticodon, pubmed-meshheading:8955898-Bacterial Proteins, pubmed-meshheading:8955898-Base Sequence, pubmed-meshheading:8955898-Carboxylic Ester Hydrolases, pubmed-meshheading:8955898-Escherichia coli, pubmed-meshheading:8955898-Methionine-tRNA Ligase, pubmed-meshheading:8955898-Models, Molecular, pubmed-meshheading:8955898-Molecular Sequence Data, pubmed-meshheading:8955898-Nucleic Acid Conformation, pubmed-meshheading:8955898-Peptide Elongation Factor Tu, pubmed-meshheading:8955898-Peptide Initiation Factors, pubmed-meshheading:8955898-Prokaryotic Initiation Factor-2, pubmed-meshheading:8955898-Prokaryotic Initiation Factor-3, pubmed-meshheading:8955898-Protein Biosynthesis, pubmed-meshheading:8955898-RNA, Messenger, pubmed-meshheading:8955898-RNA, Transfer, Met, pubmed-meshheading:8955898-Ribosomes, pubmed-meshheading:8955898-Software
pubmed:year
1996
pubmed:articleTitle
Molecular recognition governing the initiation of translation in Escherichia coli. A review.
pubmed:affiliation
Laboratoire de Biochimie, URA-CNRS no 1970, Ecole Polytechnique, Palaiseau, France.
pubmed:publicationType
Journal Article, Review