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Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions
Author(s) -
He Yingbo,
Tang Huadong,
Yi Zhiwei,
Zhou Hao,
Luo Yongzhang
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.01.059
Subject(s) - fibrillogenesis , chemistry , sequence (biology) , biophysics , fibril , mutant , yeast , urea , saccharomyces cerevisiae , biochemistry , protein aggregation , crystallography , biology , gene
To examine the effect of aggregation sequence QGGYQQQYNP from yeast Sup35 on fibril formation of sperm whale apomyoglobin (apoMb), we constructed several mutants via substitution. Urea‐induced unfolding of apoMb confirms that the substitution of the aggregation sequence does not significantly affect the stability of the mutants compared to wild type (WT) at pH 4.2. Under this condition, however, despite the difference in rate most apoMb mutants form fibrils more readily than WT with distinct morphology. These results suggest that the aggregation sequence facilitates fibril assembly of apoMb at acidic pH in vitro and this facilitation depends on the regions replaced.