Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins

Tatsuya Niwa, Bei Wen Ying, Katsuyo Saito, Wenzhen Jin, Shoji Takada, Takuya Ueda*, Hideki Taguchi

*この研究の対応する著者

研究成果: Article査読

170 被引用数 (Scopus)

抄録

Protein folding often competes with intermolecular aggregation, which in most cases irreversibly impairs protein function, as exemplified by the formation of inclusion bodies. Although it has been empirically determined that some proteins tend to aggregate, the relationship between the protein aggregation propensities and the primary sequences remains poorly understood. Here, we individually synthesized the entire ensemble of Escherichia coli proteins by using an in vitro reconstituted translation system and analyzed the aggregation propensities. Because the reconstituted translation system is chaperone-free, we could evaluate the inherent aggregation propensities of thousands of proteins in a translation-coupled manner. A histogram of the solubilities, based on data from 3,173 translated proteins, revealed a clear bimodal distribution, indicating that the aggregation propensities are not evenly distributed across a continuum. Instead, the proteins can be categorized into 2 groups, soluble and aggregation-prone proteins. The aggregation propensity is most prominently correlated with the structural classification of proteins, implying that the prediction of aggregation propensity requires structural information about the protein.

本文言語English
ページ(範囲)4201-4206
ページ数6
ジャーナルProceedings of the National Academy of Sciences of the United States of America
106
11
DOI
出版ステータスPublished - 2009 3月 17
外部発表はい

ASJC Scopus subject areas

  • 一般

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