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Mechanisms of cellular proteostasis: insights from single molecule approaches (226.3)
Author(s) -
Bustamante Carlos,
Kaiser Chrisian,
Tinoco Ignacio,
Goldman Dan
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.226.3
Subject(s) - proteostasis , proteome , biogenesis , microbiology and biotechnology , ribosome , proteases , protein folding , co chaperone , foldase , biology , ribosome biogenesis , folding (dsp implementation) , chaperone (clinical) , computational biology , chemistry , biochemistry , rna , heat shock protein , enzyme , groel , hsp70 , medicine , engineering , escherichia coli , pathology , electrical engineering , gene
Cells employ a variety of strategies to maintain the proteome homeostasis. Beginning during protein biogenesis, the ribosome itself and a number of molecular chaperones promote correct de novo folding of nascent proteins even before synthesis is complete. Another set of molecular chaperones helps to maintain proteins in their functional, native state. Polypeptides that are no longer needed or pose a threat to the cell, such as misfolded proteins and aggregates, are removed in an efficient and timely fashion by ATP‐dependent proteases. In this talk I will describe how the application of single‐molecule methods, in particular optical tweezers, is shedding new light on the molecular mechanisms of quality control during the life cycle of proteins.