Pathogenesis of bacterial infections and immunity

@article{,

title = {Bacterial translational control at atomic resolution},

author = {P Romby and M Springer},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12615010},

isbn = {12615010},

year  = {2003},

date = {2003-01-01},

journal = {Trends Genet},

volume = {19},

number = {3},

pages = {155-161},

abstract = {Translational regulation allows rapid adaptation of protein synthesis to environmental conditions. In prokaryotes, the synthesis of many RNA-binding proteins is regulated by a translational feedback mechanism involving a competition between their natural substrate and their binding site on mRNA, which are often thought to resemble each other. This article describes the case of threonyl-tRNA synthetase, which represses the translation of its own mRNA. Recent data provide the first opportunity to describe at the atomic level both the extent and the limit of mimicry between the way this enzyme recognizes tRNA(Thr) and its regulatory site in mRNA. The data also give some clues about how the binding of the synthetase to its mRNA inhibits translation.},

note = {0168-9525 

Journal Article 

Review 

Review, Tutorial},

keywords = {Bacterial  *Gene Expression Regulation, Bacterial  Models, Base Sequence  Conserved Sequence  Escherichia coli/*enzymology/*genetics  *Gene Expression Regulation, Biological  Models, Enzymologic  Genes, Genetic, Messenger/genetics/*metabolism  RNA, Molecular  Molecular Mimicry  Nucleic Acid Conformation  Operator Regions (Genetics)  RNA, Non-U.S. Gov't  Threonine-tRNA Ligase/chemistry/*genetics/metabolism  *Translation, ROMBY, Thr/*metabolism  RNA-Binding Proteins/metabolism  Support, Transfer, Unité ARN},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Yeast aspartyl-tRNA synthetase binds specifically its own mRNA},

author = {M Frugier and R Giege},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12888345},

isbn = {12888345},

year  = {2003},

date = {2003-01-01},

journal = {J Mol Biol},

volume = {331},

number = {2},

pages = {375-383},

abstract = {Dimeric class II aspartyl-tRNA synthetase (AspRS) from yeast has a modular architecture and includes an N-terminal appendix of 70 amino acid residues that protrudes from the anticodon-binding module. This extension, of predicted helical structure, is not essential for aminoacylation but contains an RNA-binding motif that promotes non-specific interactions with tRNAs. As shown here, this protein extension can also interact with the 5' end of the AspRS mRNA. In vitro, optimal binding occurs on an mRNA domain comprising part of the 87 nucleotide long 5'UTR and the sequence encoding the N-terminal appendix. At the protein side, only the appendix and the anticodon-binding module participate in the interaction between AspRS and the mRNA domain. Binding is specific, since only tRNA(Asp) can dissociate the complex. In vivo, AspRS also binds specifically this mRNA domain and in doing so triggers a reduced translation of a fused GFP mRNA. From that, a mechanism for the regulation of this eukaryotic aminoacyl-tRNA synthetase is proposed. Implications for aspartylation accuracy in yeast are given.},

note = {0022-2836 

Journal Article},

keywords = {5' Untranslated Regions  Amino Acid Motifs  Aspartate-tRNA Ligase/*chemistry/metabolism  Binding, Competitive  Blotting, Drug  Gene Expression Regulation, Enzymologic  Genes, FRUGIER, Fungal  Kinetics  Luminescent Proteins/metabolism  Plasmids  Protein Binding  Protein Structure, Messenger/metabolism  RNA, Non-U.S. Gov't, Tertiary  RNA/metabolism  RNA, Transfer/metabolism  Saccharomyces cerevisiae/metabolism  Support, Unité ARN, Western  Dose-Response Relationship},

pubstate = {published},

tppubtype = {article}

}