The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104
نویسندگان
چکیده
منابع مشابه
Differences in the Curing of [PSI+] Prion by Various Methods of Hsp104 Inactivation
[PSI(+)] yeast, containing the misfolded amyloid conformation of Sup35 prion, is cured by inactivation of Hsp104. There has been controversy as to whether inactivation of Hsp104 by guanidine treatment or by overexpression of the dominant negative Hsp104 mutant, Hsp104-2KT, cures [PSI(+)] by the same mechanism- inhibition of the severing of the prion seeds. Using live cell imaging of Sup35-GFP, ...
متن کاملCuring of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.
Propagation of the yeast prion [PSI+], a self-replicating aggregated form of Sup35p, requires Hsp104. One model to explain this phenomenon proposes that, in the absence of Hsp104, Sup35p aggregates enlarge but fail to replicate thus becoming diluted out as the yeast divide. To test this model, we used live imaging of Sup35p-GFP to follow the changes that occur in [PSI+] cells after the addition...
متن کاملHow azide inhibits ATP hydrolysis by the F-ATPases.
In the structure of bovine F1-ATPase determined at 1.95-A resolution with crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate, and azide, the azide anion interacts with the beta-phosphate of ADP and with residues in the ADP-binding catalytic subunit, betaDP. It occupies a position between the catalytically essential amino acids, beta-Lys-162 in the P loop and the "arginine finge...
متن کاملAntagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.
The maintenance of [PSI], a prion-like form of the yeast release factor Sup35, requires a specific concentration of the chaperone protein Hsp104: either deletion or overexpression of Hsp104 will cure cells of [PSI]. A major puzzle of these studies was that overexpression of Hsp104 alone, from a heterologous promoter, cures cells of [PSI] very efficiently, yet the natural induction of Hsp104 wit...
متن کاملStructure of proteins unfolded by guanidinium chloride
Small-angle neutron scattering measurements were performed on two very different proteins unfolded by guanidinium chloride. It is shown that the neutron spectra given by unfolded phosphoglycerate kinase and p-casein are similar to those of excluded volume homopolymer chains. INTRODUCTION A functional native protein generally adopts a specific three-dimensional structure that is determined by it...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m312403200