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Genomic and functional analyses reveal a distinct chaperone network linked to protein biosynthesis in eukaryotic cells
Author(s) -
Frydman Judith
Publication year - 2006
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.20.5.a890-b
Subject(s) - ribosome biogenesis , chaperone (clinical) , biogenesis , co chaperone , protein folding , ribosome , biology , protein biosynthesis , microbiology and biotechnology , translation (biology) , protein aggregation , computational biology , genetics , hsp90 , gene , heat shock protein , rna , messenger rna , medicine , pathology
Molecular chaperones assist the folding of newly translated and stress‐denatured proteins. In prokaryotes, overlapping sets of chaperones mediate both processes. In contrast, we find here that eukaryotes have evolved distinct chaperone networks to carry out these functions. A systems approach combining genomic and functional analyses indicate that in addition to stress‐inducible chaperones, which protect cells from environmental stress, eukaryotes contain a stress‐repressed chaperone network that is dedicated to protein biogenesis. These stress‐repressed chaperones are transcriptionally, functionally and physically linked to the translational apparatus and associate with nascent polypeptides emerging from the ribosome. Consistent with a function in de novo protein folding, impairment of the translation‐linked chaperone network renders cells sensitive to misfolding in the context of protein synthesis but not in the context of environmental stress. The emergence of a translation‐linked chaperone network likely underlies the elaborate co‐translational folding process necessary for the evolution of larger multidomain proteins characteristic of eukaryotic cells. Supported by NIH GM56433