Ontology highlight
ABSTRACT:
SUBMITTER: Uemura E
PROVIDER: S-EPMC5766493 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Uemura Eri E Niwa Tatsuya T Minami Shintaro S Takemoto Kazuhiro K Fukuchi Satoshi S Machida Kodai K Imataka Hiroaki H Ueda Takuya T Ota Motonori M Taguchi Hideki H
Scientific reports 20180112 1
A subset of the proteome is prone to aggregate formation, which is prevented by chaperones in the cell. To investigate whether the basic principle underlying the aggregation process is common in prokaryotes and eukaryotes, we conducted a large-scale aggregation analysis of ~500 cytosolic budding yeast proteins using a chaperone-free reconstituted translation system, and compared the obtained data with that of ~3,000 Escherichia coli proteins reported previously. Although the physicochemical prop ...[more]