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2017 ; 37
(20
): ä Nephropedia Template TP
gab.com Text
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English Wikipedia
Analysis of Small Critical Regions of Swi1 Conferring Prion Formation,
Maintenance, and Transmission
#MMPMID28716950
Valtierra S
; Du Z
; Li L
Mol Cell Biol
2017[Oct]; 37
(20
): ä PMID28716950
show ga
Saccharomyces cerevisiae contains several prion elements, which are
epigenetically transmitted as self-perpetuating protein conformations. One such
prion is [SWI(+) ], whose protein determinant is Swi1, a subunit of the SWI/SNF
chromatin-remodeling complex. We previously reported that [SWI(+) ] formation
results in a partial loss-of-function phenotype of poor growth in nonglucose
medium and abolishment of multicellular features. We also showed that the first
38 amino acids of Swi1 propagated [SWI(+)]. We show here that a region as small
as the first 32 amino acids of Swi1 (Swi1(1-32)) can decorate [SWI(+)]
aggregation and stably maintain and transmit [SWI(+)] independently of
full-length Swi1. Regions smaller than Swi1(1-32) are either incapable of
aggregation or unstably propagate [SWI(+)]. When fused to Sup35MC, the [PSI(+) ]
determinant lacking its PrD, Swi1(1-31) and Swi1(1-32) can act as transferable
prion domains (PrDs). The resulting fusions give rise to a novel chimeric prion,
[SPS(+)], exhibiting [PSI(+)]-like nonsense suppression. Thus, an NH(2)-terminal
region of ?30 amino acids of Swi1 contains all the necessary information for in
vivo prion formation, maintenance, and transmission. This PrD is unique in size
and composition: glutamine free, asparagine rich, and the smallest defined to
date. Our findings broaden our understanding of what features allow a protein
region to serve as a PrD.
|*Gene Expression Regulation, Fungal
[MESH]
|Acyltransferases/genetics/*metabolism
[MESH]
|Chromatin Assembly and Disassembly/*physiology
[MESH]