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Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP‐dependent manner
Author(s) -
Inoue Yuji,
KawaiNoma Shigeko,
KoikeTakeshita Ayumi,
Taguchi Hideki,
Yoshida Masasuke
Publication year - 2011
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2011.01510.x
Subject(s) - yeast , biology , amyloid (mycology) , saccharomyces cerevisiae , fibril , biochemistry , mutant , microbiology and biotechnology , gene , botany
We report a new type of interaction between two yeast prion proteins, Sup35 and New1. New1 consists of an N‐terminal prion region (New1N) and a C‐terminal region homologous to a translation elongation factor with two ATP‐binding motifs. Amyloid formation of the Sup35 prion region (Sup35NM) was accelerated by a small amount of sonicated New1N amyloid (New1N‐seeds) to produce Sup35NM[New1] amyloid. New1N amyloid formation was accelerated by Sup35NM[New1]‐seeds but not by spontaneously generated Sup35NM‐seeds, indicating that the structural features of the New1N amyloid were transmitted via the Sup35NM amyloid. Surprisingly, full‐length New1 broke the Sup35NM amyloid fibrils in an ATP‐dependent manner. This activity of New1 was independent from Hsp104. It was lost by a mutation in the second ATP‐binding motif, by the truncation of the N‐terminal prion region of New1 and by the pre‐incubation of New1 with New1N‐seeds. When New1 was overproduced in yeast [ PSI + ] cells carrying GFP‐fused Sup35NM, diverse morphological changes in fluorescent foci occurred. Thus, New1 potentially has a regulatory role in prion state in yeast, working independently of the Hsp104 system.