ARN

@article{,

title = {Structure-function insights into prokaryotic and eukaryotic translation initiation},

author = {A G Myasnikov and A Simonetti and S Marzi and B P Klaholz},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19493673},

isbn = {19493673},

year  = {2009},

date = {2009-01-01},

journal = {Curr Opin Struct Biol},

volume = {19},

number = {3},

pages = {300-9},

abstract = {Translation initiation is the rate-limiting and most complexly regulated step of protein synthesis in prokaryotes and eukaryotes. In the last few years, cryo-electron microscopy has provided several novel insights into the universal process of translation initiation. Structures of prokaryotic 30S and 70S ribosomal initiation complexes with initiator transfer RNA (tRNA), messenger RNA (mRNA), and initiation factors have recently revealed the mechanism of initiator tRNA recruitment to the assembling ribosomal machinery, involving molecular rearrangements of the ribosome and associated factors. First three-dimensional pictures of the particularly complex eukaryotic translation initiation machinery have been obtained, revealing how initiation factors tune the ribosome for recruiting the mRNA. A comparison of the available prokaryotic and eukaryotic structures shows that--besides significant differences--some key ribosomal features are universally conserved.},

note = {1879-033X (Electronic) 

0959-440X (Linking) 

Journal Article 

Research Support, Non-U.S. Gov't 

Review},

keywords = {Amino Acid Sequence Eukaryotic Cells/*chemistry/*metabolism Humans Molecular Sequence Data *Peptide Chain Initiation, mino Acid Sequence Eukaryotic Cells/*chemistry/*metabolism Humans Molecular Sequence Data *Peptide Chain Initiation, ROMBY, Transfer/chemistry/metabolism  Ribosomes/chemistry/genetics/metabolism, Translational  Peptide Initiation Factors/chemistry/metabolism  Prokaryotic Cells/*chemistry/*metabolism  RNA, Unité ARN},

pubstate = {published},

tppubtype = {article}

}