A Small, Glutamine-Free Domain Propagates the [<i>SWI</i><sup>+</sup>] Prion in Budding Yeast

Crow, Emily T.; Du, Zhiqiang; Li, Liming

doi:10.1128/mcb.05338-11

Cited by 21 publications

(18 citation statements)

References 56 publications

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“…We recently found that this prion too appears commonly in wild strains, allowing cells to respond to their ecological niche in a heritable way (D. F. Jarosz, J. C. S. Brown, G. A. Walker, A. K. Lancaster, L. F. Bisson and S.L., unpublished observations). Other prions alter the activity of chromatin-remodelling factors 54,84 , prevent fungi from out-crossing 85 or alter antibiotic resistance 60,86 . In other words, they alter the biology of the organism in fundamental ways.…”

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confidence: 99%

Transgenerational epigenetic inheritance: how important is it?

et al. 2013

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Much attention has been given to the idea of transgenerational epigenetic inheritance, but fundamental questions remain regarding how much takes place and the impact that this might have on organisms. We asked five leading researchers in this area — working on a range of model organisms and in human disease — for their views on these topics. Their responses highlight the mixture of excitement and caution that surrounds transgenerational epigenetic inheritance and the wide gulf between species in terms of our knowledge of the mechanisms that may be involved.

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confidence: 99%

Transgenerational epigenetic inheritance: how important is it?

et al. 2013

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“…This is a currently expanding field, with several new examples of functional yeast prions reported including Swi1p, a part of the SWI/SNF chromatin-remodeling complex that is involved in regulation of 6% of the genes in S. cerevisiae . Aggregation of Swi1p alters the regulation of the complex and is transmitted to offspring by the cytoplasm [84,85]. Therefore, amyloid aggregation can significantly impact fungal physiology, while also imparting inheritable changes.…”

Section: Functional Amyloids In Epigenetic Inheritancementioning

confidence: 99%

Diversity, biogenesis and function of microbial amyloids

Blanco

Evans

Smith

et al. 2012

Trends in Microbiology

285

266

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Amyloid is a distinct β-sheet-rich fold that many proteins can acquire. Frequently associated with neurodegenerative diseases in humans, including Alzheimer’s, Parkinson’s and Huntington’s, amyloids are traditionally considered the product of protein misfolding. However, the amyloid fold is now recognized as a ubiquitous part of normal cellular biology. ‘Functional’ amyloids have been identified in nearly all facets of cellular life, with microbial functional amyloids leading the way. Unlike disease-associated amyloids, functional amyloids are assembled by dedicated, directed pathways and ultimately perform a physiological function that benefits the organism. The evolved amyloid assembly and disassembly pathways of microbes have provided novel insights into how cells have harnessed the amyloid assembly process for productive means. Understanding functional amyloid biogenesis promises to provide a fresh perspective on the molecular events that underlie disease-associated amyloidogenesis. Here, we review functional microbial amyloids with an emphasis on curli fibers and their role in promoting biofilm formation and other community behaviors.

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“…Typically, they are more N-than Q-rich (e.g., Alberti et al 2009), and "minimal" PrDs may contain no Qs (Crow et al 2011). Substitution of Qs for Ns increases, while substitution of Ns for Qs decreases, prion propagation by a given protein (Halfmann et al 2011).…”

Section: Prion Domainsmentioning

confidence: 99%

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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A Small, Glutamine-Free Domain Propagates the [SWI⁺] Prion in Budding Yeast

Cited by 21 publications

References 56 publications

Transgenerational epigenetic inheritance: how important is it?

Transgenerational epigenetic inheritance: how important is it?

Diversity, biogenesis and function of microbial amyloids

Prions in Yeast

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A Small, Glutamine-Free Domain Propagates the [SWI+] Prion in Budding Yeast

Cited by 21 publications

References 56 publications

Transgenerational epigenetic inheritance: how important is it?

Transgenerational epigenetic inheritance: how important is it?

Diversity, biogenesis and function of microbial amyloids

Prions in Yeast

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Product

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A Small, Glutamine-Free Domain Propagates the [SWI⁺] Prion in Budding Yeast