Figures and figure supplements Hsp 70 - associated chaperones have a critical role in buffering protein production costs Zoltán

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  • Zoltán Farkas
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Hsp70-associated chaperones have a critical role in buffering protein production costs

Proteins are necessary for cellular growth. Concurrently, however, protein production has high energetic demands associated with transcription and translation. Here, we propose that activity of molecular chaperones shape protein burden, that is the fitness costs associated with expression of unneeded proteins. To test this hypothesis, we performed a genome-wide genetic interaction screen in bak...

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Chaperone-assisted protein folding in the cell cytoplasm.

Folding of polypeptides in the cell typically requires the assistance of a set of proteins termed molecular chaperones. Chaperones are an essential group of proteins necessary for cell viability under both normal and stress conditions. There are several chaperone systems which carry out a multitude of functions all aimed towards insuring the proper folding of target proteins. Chaperones can ass...

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Ribosome-associated chaperones as key players in proteostasis.

De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperones. Besides cytosolic and organelle-specific chaperones, cells have evolved ribosome-associated chaperones that support early folding events and prevent misfolding and aggregation. This class of chaperones includes the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-...

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Hsp 104 , Hsp 70 , and Hsp 40 : A Novel Chaperone System that Rescues Previously Aggregated

are involved in protein turnover. Neither ClpA nor ClpX Hsp104 is a stress tolerance factor that promotes the has intrinsic proteolytic activity. Rather, both proteins reactivation of heat-damaged proteins in yeast by an confer ATP-dependent turnover of their substrates unknown mechanism. Herein, we demonstrate that through a physical association with an unrelated oligoHsp104 functions in this ...

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Protein folding: Chaperones get Hip

In the cell, nascent and completed polypeptides may misfold and aggregate. A class of proteins called molecular chaperones has evolved to facilitate the production of native, functional forms of proteins. These chaperones also aid in the translocation of proteins across biological membranes. The ubiquitous heat-shock protein (Hsp) 70 class of chaperones has been the subject of intensive study o...

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تاریخ انتشار 2018