Discrete roles of trehalose and Hsp104 in inhibition of protein aggregation in yeast cells.

Abstract:

:Heat shock response (HSR) is an important element of cellular homeostasis. In yeast, HSR comprises of the heat shock proteins (Hsps) and the osmolytes trehalose and glycerol. The respective roles of trehalose and Hsp104 in regulating protein aggregation remain ambiguous. We report that trehalose and Hsp104 are important during the early stages of protein aggregation, i.e. when the process is still reversible. This corroborates the earlier reported role of trehalose being an inhibitor of protein folding. Under in vitro conditions, trehalose is able to restore the GdHCl-induced loss of ATPase activity of recombinant Hsp104 to almost its original level. As the saturation phase of aggregation approaches, neither of the two components is able to exert any effect. Inactivation of Hsp104 at the stage when oligomers have already been formed increases the rate of formation of aggregates by inhibiting disaggregation of oligomers. In the absence of an active disaggregase, the oligomers are converted to mature irreversible aggregates, accelerating their formation. Our results suggest that the disaccharide may have a marginally stronger influence than Hsp104 in inhibiting protein aggregation in yeast cells.

journal_name

FEMS Yeast Res

journal_title

FEMS yeast research

authors

Sethi R,Iyer SS,Das E,Roy I

doi

10.1093/femsyr/foy058

subject

Has Abstract

pub_date

2018-09-01 00:00:00

issue

6

eissn

1567-1356

issn

1567-1364

pii

5025658

journal_volume

18

pub_type

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