30
September 2004
Ribosomes: exit strategy
While being synthesized on the ribosome, proteins fold into their functional three-dimensional structure as they emerge into the cytosol. At this time they are particularly vulnerable to aggregation and proteolysis, but ribosome-associated chaperones and factors interact with the nascent polypeptide to facilitate protein folding. A high-resolution structural study of the complex between a ribosome and a ribosome-associated chaperone reveals that a nascent peptide is synthesized into a well defined protective molecular cage formed between the ribosomal exit tunnel and the chaperone. These results provide structural understanding of a fundamental cellular process.
Trigger factor in complex with the ribosome
forms a molecular cradle for nascent proteins
LARS FERBITZ, TIMM MAIER, HOLGER PATZELT, BERND BUKAU,
ELKE DEUERLING & NENAD BAN
Nature AOP published online 29 August 2004; doi:10.1038/nature02899
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Cell biology: Sight at the end of the tunnel
ARTHUR HORWICH
A chaperone molecule called trigger factor binds new polypeptide chains
as they emerge from the protein-synthesis machinery. Crystal structures
suggest that this molecule forms a hydrophobic 'cradle'.
Nature 431, 520–522 (2004); doi:10.1038/431520a
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