Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo‐dimer with topologically interlinked chains. Issue 2 (25th January 2016)

• Record Type: Journal Article
• Authors: Aguirre, César; Goto, Yuji; Costas, Miguel
• Is Part Of: FEBS letters. Volume 590:Issue 2(2016)
• Page Start: 202
• Page End: 214
• Publication Date: 2016-01-25
• Subjects: entangled chains -- interlinked chains -- PaSdsA1 sulfatase -- stabilization with SDS -- unfolding pathways; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12041
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Understanding the mechanisms as to how interlinked proteins entangle and fold is a challenge. PaSdsA1 sulfatase is a homo‐dimer containing two zinc atoms per monomer. The monomer chains are interlinked in a dimerization domain. To study the unfolding pathways denaturation experiments were performed. In the native protein three forms coexist in chemical equilibrium, each with a different number of zinc atoms. In the chemical unfolding of the holo‐dimers the entanglement of the chains is preserved and acts as a 'folding seed', allowing the unfolding process to be reversible. Thermal irreversible unfolding of the holo‐dimers favours dissociation, producing monomers that are SDS‐stabilized. The thermal unfolding of these monomers is reversible. However, it is not possible to form dimers from unfolded monomers. Abstract :