Imaging

@article{,

title = {Ribosomal protein S15 represses its own translation via adaptation of an rRNA-like fold within its mRNA},

author = {A Serganov and A Polonskaia and B Ehresmann and C Ehresmann and D J Patel},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12682022},

isbn = {12682022},

year  = {2003},

date = {2003-01-01},

journal = {EMBO J},

volume = {22},

number = {8},

pages = {1898-1908},

abstract = {The 16S rRNA-binding ribosomal protein S15 is a key component in the assembly of the small ribosomal subunit in bacteria. We have shown that S15 from the extreme thermophile Thermus thermophilus represses the translation of its own mRNA in vitro, by interacting with the leader segment of its mRNA. The S15 mRNA-binding site was characterized by footprinting experiments, deletion analysis and site-directed mutagenesis. S15 binding triggers a conformational rearrangement of its mRNA into a fold that mimics the conserved three-way junction of the S15 rRNA-binding site. This conformational change masks the ribosome entry site, as demonstrated by direct competition between the ribosomal subunit and S15 for mRNA binding. A comparison of the T.thermophilus and Escherichia coli regulation systems reveals that the two regulatory mRNA targets do not share any similarity and that the mechanisms of translational inhibition are different. Our results highlight an astonishing plasticity of mRNA in its ability to adapt to evolutionary constraints, that contrasts with the extreme conservation of the rRNA-binding site.},

note = {0261-4189 

Journal Article},

keywords = {Bacterial Proteins/genetics/metabolism  Binding Sites  *Nucleic Acid Conformation  Protein Binding  Protein Footprinting  RNA, Genetic, Messenger/chemistry/*metabolism  Repressor Proteins/genetics/*metabolism  Ribosomal Proteins/genetics/*metabolism  Ribosomes/metabolism  Support, P.H.S.  Thermus thermophilus/genetics/metabolism  *Translation, U.S. Gov't, Unité ARN},

pubstate = {published},

tppubtype = {article}

}