Grimani

Talbot, Michael

doi:10.1093/gmo/9781561592630.article.40663

Cited by 1 publication

(2 citation statements)

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“…Nucleic acid extraction was performed using standard cetyl trimethyl ammonium bromide (CTAB) extraction techniques as previously described (Talbot and Talbot, 2001). Subsequent PCR, gel electrophoresis, and restriction enzyme digests were carried out under standard procedures (Sambrook and Russell, 2001).…”

Section: Nucleic Acid Isolations and Analysismentioning

confidence: 99%

“…Fungal transformation was carried out on protoplasts using an established protocol (Talbot and Talbot, 2001). To generate strains ex-pressing Hsp104-GFP and Hsp104 DWB -GFP, we first deleted the endogenous copy of HSP104 by replacement with a selectable marker conferring resistance to hygromycin B, using a split marker approach (Catlett et al, 2003).…”

Section: Fungal Transformationmentioning

confidence: 99%

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Autophagy machinery promotes the chaperone-mediated formation and compartmentalization of protein aggregates during appressorium development by the rice blast fungus

Rogers

Egan

2020

MBoC

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The chaperone-mediated sequestration of misfolded proteins into specialized quality control compartments represents an important strategy for maintaining protein homeostasis in response to stress. However, precisely how this process is controlled in time and subcellular space and integrated with the cell's protein refolding and degradation pathways, remains unclear. We set out to understand how aggregated proteins are managed during infection-related development by a globally devastating plant pathogenic fungus, and to determine how impaired protein quality control impacts upon cellular differentiation and pathogenesis in this system. Here we show that in the absence of Hsp104 disaggregase activity aggregated proteins are spatially sequestered into quality control compartments within conidia, but not within terminally differentiated infection cells, and thus spatial protein quality control is cell-type dependent. We demonstrate that impaired aggregate resolution results in a short-term developmental penalty but has no significant impact upon appressorium function. Lastly, we show that, somewhat unexpectedly, the autophagy machinery is necessary for the normal formation and compartmentalization of protein aggregates. Taken together, our findings provide important new insight into spatial protein quality control during the process of terminal cellular differentiation by a globally important model eukaryote and reveals a new level of interplay between major proteostasis pathways. [Media: see text]

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Section: Nucleic Acid Isolations and Analysismentioning

confidence: 99%

Section: Fungal Transformationmentioning

confidence: 99%