Molecular guardians for newborn proteins: ribosome-associated chaperones and their role in protein folding |
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Authors: | R D Wegrzyn E Deuerling |
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Institution: | 1. Zentrum für Molekulare Biologie (ZMBH), Universit?t Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany
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Abstract: | A central dogma in biology is the conversion of genetic information into active proteins. The biosynthesis of proteins by
ribosomes and the subsequent folding of newly made proteins represent the last crucial steps in this process. To guarantee
the correct folding of newly made proteins, a complex chaperone network is required in all cells. In concert with ongoing
protein biosynthesis, ribosome-associated factors can interact directly with emerging nascent polypeptides to protect them
from degradation or aggregation, to promote folding into their native structure, or to otherwise contribute to their folding
program. Eukaryotic cells possess two major ribosome-associated systems, an Hsp70/Hsp40-based chaperone system and the functionally
enigmatic NAC complex, whereas prokaryotes employ the Trigger Factor chaperone. Recent structural insights into Trigger Factor
reveal an intricate cradle-like structure that, together with the exit site of the ribosome, forms a protected environment
for the folding of newly synthesized proteins.
Received 29 June 2005; received after revision 4 August 2005; accepted 18 August 2005 |
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Keywords: | Trigger Factor Ssb Zuotin NAC co-translational protein folding ribosome |
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