Chaperonin-encapsulation of proteins for NMR.

• Tanaka, Shinji

• Kawata, Yasushi

• Otting, Gottfried

• Dixon, Nicholas E

• Matsuzaki, Katsumi

• Hoshino, Masaru

Abstract

A novel chaperonin-encapsulation system for NMR measurements has been designed. The single-ring variant SR398 with an ATPase deficient mutation of GroEL, also known as chaperonin, bound co-chaperonin GroES irreversibly, forming a stable cage to encapsulate a target protein. A small GroEL-binding tag made it possible to perform all steps of the encapsulation under near physiological conditions while retaining the native conformation of the target protein. About half of the SR398/GroES cages encapsulated target protein molecules. As binding only depends on the 12-residue tag sequence, this encapsulation method is applicable to a large number of proteins. Isolation of the target proteins in the molecular cage of chaperonin will allow the study of highly aggregation-prone proteins by solution NMR.

Journal

• Biochimica et biophysica acta

  Biochimica et biophysica acta 1804 (4), 866-871, 2010-04

  Elsevier BV

Keywords

• Aggregation
• GroE
• Molecular chaperone
• NMR
• Protein encapsulation

Details

• CRID: 1050001335654485248
• NII Article ID: 120001981960
• NII Book ID: AA00564635
• ISSN: 00063002
• HANDLE: 2433/108262
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles