Access this Article

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

Codes

  • NII Article ID (NAID)
    120001981960
  • Text Lang
    ENG
  • Article Type
    journal article
  • ISSN
    0006-3002
  • Data Source
    IR 
Page Top