The C-terminal domain of human grp94 protects the catalytic subunit of protein kinase CK2 (CK2α) against thermal aggregation: Role of disulfide bonds

Nerea Roher, Francesc Miró, Brigitte Boldyreff, Franc Llorens, Maria Plana, Olaf Georg Issinger, Emilio Itarte

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16 Citations (Scopus)

Abstract

The C-terminal domain (residues 518-803) of the 94 kDa glucose regulated protein (grp94) was expressed in Escherichia coli as a fusion protein with a His6-N-terminal tag (grp94-CT). This truncated form of grp94 formed dimers and oligomers that could be dissociated into monomers by treatment with dithiothreitol. Grp94-CT conferred protection against aggregation on the catalytic subunit of protein kinase CK2 (CK2α), although it did not protect against thermal inactivation. This anti-aggregation effect of grp94-CT was concentration dependent, with full protection achieved at grp94-CT/CK2α molar ratios of 4 : 1. The presence of dithiothreitol markedly reduced the anti-aggregation effects of grp94-CT on CK2α without altering the solubility of the chaperone. It is concluded that the chaperone activity of the C-terminal domain of human grp94 requires the maintenance of its quaternary structure (dimers and oligomers), which seems to be stabilised by disulphide bonds.
Original languageEnglish
Pages (from-to)429-436
JournalEuropean Journal of Biochemistry
Volume268
DOIs
Publication statusPublished - 1 Jan 2001

Keywords

  • Aggregation
  • Chaperone assay
  • Protein kinase CK2
  • grp94

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