Requirements of Hsp104p activity and Sis1p binding for propagation of the [<i>RNQ+</i>] prion

Bardill, J. Patrick; Dulle, Jennifer E.; Fisher, Jonathan R.; True, Heather L.

doi:10.4161/pri.3.3.9662

Cited by 18 publications

(20 citation statements)

References 63 publications

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“…Oligonucleotides used to clone the yeast plasmids are listed in Protein Analysis-Sedimentation analysis of Rnq1 was performed as described previously (27) and assessed by SDS-PAGE and Western blot using an ␣Rnq1 antibody. The total and soluble fractions were quantified using ImageJ and used to calculate the percent soluble protein.…”

Section: Methodsmentioning

confidence: 99%

Myopathy-causing Mutations in an HSP40 Chaperone Disrupt Processing of Specific Client Conformers

Stein

Bengoechea

Harms

et al. 2014

Journal of Biological Chemistry

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100

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Background: Mutations in the G/F domain of the human HSP40 chaperone DNAJB6 cause a protein aggregate myopathy. Results: Homologous mutations in the yeast HSP40 Sis1 alter prion propagation in a prion strain-dependent manner. Conclusion: G/F domain mutations affect chaperone-mediated processing of particular client conformers. Significance: Impaired processing of certain substrate conformations may be one mechanism that contributes to chaperonopathy pathogenesis.

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Section: Methodsmentioning

confidence: 99%

Myopathy-causing Mutations in an HSP40 Chaperone Disrupt Processing of Specific Client Conformers

Stein

Bengoechea

Harms

et al. 2014

Journal of Biological Chemistry

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100

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“…In fact, the presence of [RNQ+] induces de novo appearance of [PSI+] by several fold (Derkatch et al 1997, Kurahashi et al 2011). Interestingly, [RNQ+] seems to need less Hsp104 activity to maintain transmissible forms when compared to Sup35 (Bardill et al 2009) (Newnam et al 1999, Lopez et al 2003, Douglas et al 2008. In fact, all yeast prions discussed here require the presence of Sis1, but have different sensitivities to its depletion (Higurashi et al 2008, Kirkland et al 2011.…”

Section: Yeast Hsp104 a Molecular Chaperone Involved In The Recoverymentioning

confidence: 99%

Disaggregases, molecular chaperones that resolubilize protein aggregates

Mokry

Abrahão

Ramos

2015

An. Acad. Bras. Ciênc.

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The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance.

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“…In addition to facilitating prion formation, [RNQ + ] is involved in seemingly "nonproductive" prion interactions, the purpose of which is unclear. 22 This change in solubility of the Rnq1 protein in these variants is often difficult to detect, 40 however, and not as marked as the changes seen with variants of [PSI + ]. Moreover, vitro.…”

Section: The Pfd Of Rnq1p Is Complex and May Not Be Confined To The Qmentioning

confidence: 99%

The [RNQ+] prion: A model of both functional and pathological amyloid

Stein

True²

2011

Prion

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Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ+] prion

Cited by 18 publications

References 63 publications

Myopathy-causing Mutations in an HSP40 Chaperone Disrupt Processing of Specific Client Conformers

Myopathy-causing Mutations in an HSP40 Chaperone Disrupt Processing of Specific Client Conformers

Disaggregases, molecular chaperones that resolubilize protein aggregates

The [RNQ+] prion: A model of both functional and pathological amyloid

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