Database Description

General information of database
Database name	eSOL
Alternative name	Solubility database of all E.coli proteins
DOI	10.18908/lsdba.nbdc00440-000
Creator	Creator Name Tatsuya Niwa Creator Affiliation Department of Biomolecular Engineering, School and Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology Creator Name Hideaki Sugawara Creator Affiliation The Research and Development of Biological Databases Project, National Institute of Genetics Creator Name Takuya Ueda Creator Affiliation Department of Medical Genome Science, Graduate School of Frontier Sciences, The University of Tokyo Creator Name Hideki Taguchi* Creator Affiliation Department of Biomolecular Engineering, School and Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
Contact address	Hideki Taguchi Department of Biomolecular Engineering, School and Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa 226-8501 Japan Email: Tel.: +81-45-924-5785
Database classification	Protein sequence databases - Protein properties
Organism	Taxonomy Name Escherichia coli Taxonomy ID 562
Database description	The database of solubilities and synthetic yields of all E.coli proteins translated by using an in vitro reconstituted translation system. For 788 aggregation-prone proteins, the data of chaperone effects on the prevention of aggregate formation were added on May 2012. Gene segments from plasmids of ASKA library (Kitagawa et al. 2005) , which is the library of all genes of the E. coli strain K-12, were amplified by PCR, and their proteins were synthesized by using an in vitro translation system (PURE system). The solubilities were evaluated by SDS-PAGE and autoradiography before and after centrifugation. For aggregation-prone proteins (defined as the proteins with less than 30% solubility in the absence of any chaperone), observations of changes in solubility were made by adding the major chaperones of E. coli, Trigger Factor (TF), DnaK/DnaJ/GrpE (KJE) and GroEL/ES (GroE), individually.
Features and manner of utilization of database	Since PURE system is a reconstituted chaperone-free translation system, it is possible to evaluate the solubilities of translated proteins and the chaperone effects accurately. The acquired data will form the basis of protein folding studies and be useful for planning researches and industries using protein expression and improving their efficiencies.
License	CC BY-SA Detail
Background and funding	-
Reference(s)	Article title Global analysis of chaperone effects using a reconstituted cell-free translation system. Author name(s) Niwa T, Kanamori T, Ueda T, Taguchi H. Journal Proc Natl Acad Sci U S A. 2012 Jun 5;109(23):8937-42. External Links Article title Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins. Author name(s) Niwa T, Ying BW, Saito K, Jin W, Takada S, Ueda T, Taguchi H. Journal Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4201-6. External Links
Original website information
Database maintenance site	The Targeted Proteins Research Program promoted by the MEXT
URL of the original website	http://www.tanpaku.org/tp-esol/download.php?lang=en http://www.tanpaku.org/tp-esol/index.php?lang=en
Operation start date	2009/06/18
Last update date	2012/05/02
URL of the portal site	http://www.tanpaku.org/e_index.php
Whole data download	http://www.tanpaku.org/tp-esol/download.php?lang=en
Referenced database	GenoBase
Entry list	Not available
Query search	Not available
Web services	Not available
URL of Web services	-
Need for user registration	Not available