Curing of Yeast [<i>URE3</i>] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70

Sharma, Deepak; Stanley, Robert F.; Masison, Daniel C.

doi:10.1534/genetics.108.098699

Cited by 40 publications

(47 citation statements)

References 47 publications

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“…The evidence implicating Ydj1 (Moriyama et al 2000;Sharma et al 2009;Hines et al 2011) and Sis1 (see below) in prion propagation is unambiguous. As Sis1 is essential (see Rikhvanov et al 2007), its effect on prions were studied with mutants, internal deletions, or transient depletions, rather than complete disruptions.…”

Section: Role Of Other Hspsmentioning

confidence: 89%

Prions in Yeast

2012

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The concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that yeast also has heritable elements transmitted via protein. Indeed, the "protein only" model of prion transmission was first proven using a yeast prion. Typically, known prions are ordered cross-b aggregates (amyloids). Recently, there has been an explosion in the number of recognized prions in yeast. Yeast continues to lead the way in understanding cellular control of prion propagation, prion structure, mechanisms of de novo prion formation, specificity of prion transmission, and the biological roles of prions. This review summarizes what has been learned from yeast prions.

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Section: Role Of Other Hspsmentioning

confidence: 89%

Prions in Yeast

2012

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“…12 Mutagenesis of Ydj1p showed its interaction with Hsp70 is both necessary and sufficient for the curing. 48 Efficiency of this curing also depends on interaction of Ydj1p with specific Ssa Hsp70s. 49 Depleting the essential Hsp40 Sis1p causes rapid and efficient loss of [URE3] 28,30,31 Although the basis of this impairment has yet to be worked out, these findings suggest that Hsp70 and its co-chaperones contribute importantly to the mechanism of curing by overexpressed Hsp104.…”

Section: Hsp70 and Its Co-chaperonesmentioning

confidence: 99%

Modulation and elimination of yeast prions by protein chaperones and co-chaperones.

Reidy

Masison

2011

Prion

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] provided a simple and satisfying explanation for a large body of puzzling data regarding these elements. It also established yeast as a system for studying amyloid and the prion-like behavior of proteins.The yeast system has since provided much insight into various aspects of prion biology. Having the advantages of facile and powerful genetics and molecular biology, the fungal prion field was first to confirm the prion hypothesis by demonstrating that proteins alone can act as infectious agents.2-6 Meeting the genetic criteria for yeast prions defined by Wickner, several other yeast proteins also have been found to be capable of behaving as infectious proteins. Like their mammalian counterparts, the basis of the prion phenotype is the propensity of these proteins to misfold and form highly ordered fibrous aggregates called amyloid.Since prions are improperly folded proteins, it is not surprising that alterations in abundance or function of protein chaperones and co-chaperones strongly influence yeast prion propagation. Many of these factors were identified on the basis of how their overexpression or depletion affects prion phenotypes. Molecular chaperones and co-chaperones overlap functionally, interact in complex ways, and their expression is feedback regulated. Therefore, it is difficult to know how altering abundance of any one of them influences cellular chaperone activity overall or whether any influence on prions can be attributed solely to the The yeast system has provided considerable insight into the biology of amyloid and prions. Here we focus on how alterations in abundance or function of protein chaperones and co-chaperones affect propagation of yeast prions. In spite of a considerable amount of information, a clear understanding of the molecular mechanisms underlying these effects remains wanting.

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“…The Ydj1 and Sis1 cytosolic Hsp40s influence prion propagation in different ways. Over-expressing Ydj1 cures cells of [URE3], apparently though interaction with Hsp70, but does not effect [ PSI + ] [14, 113]. Depleting Sis1 causes rapid and efficient loss of [URE3] and [ PIN + ], but affects [ PSI + ] weakly and only after a very long delay, indicating [ PSI + ] prions depend less strictly on Sis1 than the other prions [114].…”

Section: Chaperone Functions Required For Amyloid-based Yeast Prionsmentioning

confidence: 99%

“…Prion aggregates also can sequester other proteins that interact with the prion proteins specifically or with aggregates in general [11–13]. Accordingly, the presence of prions can have deleterious effects on growth, especially when protein chaperone systems are compromised [14–16]. Table 2 lists the most studied yeast prions and their protein determinants, the normal cellular functions of the proteins and the phenotypes caused by sequestration of the proteins into insoluble prion fibers.…”

Section: Introductionmentioning

confidence: 99%

Yeast Prions Help Identify and Define Chaperone Interaction Networks

Reidy¹,

Masison

2014

CPB

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Proteins in the cell experience various stressful conditions that can affect their ability to attain and maintain the structural conformations they need to perform effectively. Protein chaperones are an important part of a cellular protein quality control system that protects the integrity of the proteome in the face of such challenges. Chaperones from different conserved families have multiple members that cooperate to regulate each other’s activity and produce machines that perform a variety of tasks. The large numbers of related chaperones with both functionally overlapping and distinct activities allows fine-tuning of the machinery for specific tasks, but presents a daunting degree of complexity. Yeast prions are misfolded forms of cellular proteins whose propagation depends on the action of protein chaperones. Studying how propagation of yeast prions is affected by alterations in functions of various chaperones provides an approach to understanding this complexity.

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Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70

Cited by 40 publications

References 47 publications

Prions in Yeast

Prions in Yeast

Modulation and elimination of yeast prions by protein chaperones and co-chaperones.

Yeast Prions Help Identify and Define Chaperone Interaction Networks

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