tailieunhanh - Báo cáo y học: "Distinct yet linked: chaperone networks in the eukaryotic cytosol"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Distinct yet linked: chaperone networks in the eukaryotic cytosol. | Minireview Distinct yet linked chaperone networks in the eukaryotic cytosol Sabine Rospert and Agnieszka Chacinska Address Institute of Biochemistry and Molecular Biology University of Freiburg Hermann-Herder-Strasse 7 D-79104 Freiburg Germany. Correspondence Sabine Rospert. Email Published 31 March 2006 Genome Biology 2006 7 208 doi gb-2006-7-3-208 The electronic version of this article is the complete one and can be found online at http 2006 7 3 208 2006 BioMed Central Ltd Abstract The terms chaperone and heat-shock protein are frequently used as synonyms but this is an oversimplification. Although one subset of chaperones is induced by heat stress a distinct group fails to respond in the same manner. Recent work reveals that this latter group is linked to the translational apparatus and functions in co-translational processes. A decade ago it was recognized that chaperone systems in bacteria form a lateral network of cooperating proteins 1 . The idea of chaperones acting in parallel with the capacity to replace each other turned out to be a best-seller and is now generally accepted. Recent work by Albanese et al. 2 in the yeast Saccharomyces cerevisiae now modifies this concept and suggests the existence of distinct and independent chaperone networks in eukaryotes. One network consists of heat-inducible chaperones that can rescue or dispose of proteins in response to various environmental stresses. The other is thought to be required specifically during de novo protein folding. A chaperone is not always a heat-shock protein as well Some years ago Brown and co-workers 3 analyzed the transcriptional profiles of yeast in response to environmental changes including a variety of stress conditions. Now Albanese et al. 2 have performed clustering analysis of these datasets for chaperone-encoding genes discovering that transcription of a defined group is co-regulated with the 138 yeast ribosomal protein

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