Toward an understanding of the structural basis of translation 英文参考文献.docVIP

Review Toward an understanding of the structural basis of translation Joachim Frank Address: Howard Hughes Medical Institute, Health Research, Inc., at the Wadsworth Center and Department of Biomedical Sciences, State University of New York at Albany, Empire State Plaza, Albany, NY 12201-0509, USA. E-mail: Joachim@ Published: 19 November 2003 Genome Biology 2003, 4:237 The electronic version of this article is the complete one and can be found online at /2003/4/12/237 ? 2003 BioMed Central Ltd Abstract The recently solved X-ray crystal structures of the ribosome have provided opportunities for studying the molecular basis of translation with a variety of methods including cryo-electron microscopy - where maps give the first glimpses of ribosomal evolution - and fluorescence spectroscopy techniques. The bacterial ribosome, a 2.5 MDa assembly formed by three large RNA molecules and 51 proteins, is the most complex biological structure that is currently known at atomic resolu- tion. It is surpassed by some large viruses in sheer number of atoms (250,000 in the ribosome, if we include the hydro- gen atoms), but such viruses are typically formed by sym- metrically arranged repeats of a unique structure whose size is easily dwarfed by the ribosome, which has no repeated units. The ribosome’s function - to translate the genetic code into protein - is one of the most fundamental processes of life, and intense efforts are going into elucidating the under- lying mechanisms. These efforts are reminiscent of the heroic struggle to solve another of life’s riddles, the question of how genetic information is stored and replicated, which resulted in the discovery of the structure of DNA 50 years ago. A review of research on the ribosome from its discovery in 1957 until the turn of the century is found in Spirin’s com- prehensive book [1]. and elongation factors Tu (EF-Tu [7]) and G (