Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells

@article{citeulike:474195, abstract = {SummaryMolecular chaperones assist the folding of newly translated and stress-denatured proteins. In prokaryotes, overlapping sets of chaperones mediate both processes. In contrast, we find that eukaryotes evolved distinct chaperone networks to carry out these functions. Genomic and functional analyses indicate that in addition to stress-inducible chaperones that protect the cellular proteome from 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 cotranslational folding process necessary for the evolution of larger multidomain proteins characteristic of eukaryotic cells.}, author = {Albanese, Veronique and Yam, Alice Y. and Baughman, Joshua and Parnot, Charles and Frydman, Judith }, citeulike-article-id = {474195}, doi = {http://dx.doi.org/10.1016/j.cell.2005.11.039}, journal = {Cell}, keywords = {clip, sis1, ssb1}, month = {January}, number = {1}, pages = {75--88}, posted-at = {2007-01-10 17:19:53}, priority = {2}, title = {Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells}, url = {http://dx.doi.org/10.1016/j.cell.2005.11.039}, volume = {124}, year = {2006} }

TY - JOUR ID - citeulike:474195 L3 - citeulike-article-id:474195 TI - Systems Analyses Reveal Two Chaperone Networks with Distinct Functions in Eukaryotic Cells JF - Cell VL - 124 IS - 1 SP - 75 EP - 88 N2 - SummaryMolecular chaperones assist the folding of newly translated and stress-denatured proteins. In prokaryotes, overlapping sets of chaperones mediate both processes. In contrast, we find that eukaryotes evolved distinct chaperone networks to carry out these functions. Genomic and functional analyses indicate that in addition to stress-inducible chaperones that protect the cellular proteome from 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 cotranslational folding process necessary for the evolution of larger multidomain proteins characteristic of eukaryotic cells. KW - clip KW - sis1 KW - ssb1 AU - Albanese, Veronique AU - Yam, Alice AU - Baughman, Joshua AU - Parnot, Charles AU - Frydman, Judith PY - 2006/01/13/ UR - http://dx.doi.org/10.1016/j.cell.2005.11.039 ER -