To establish whether the species-specific variations at the subunit interface of bacterial Cu,Zn superoxide dismutases affect dimer assembly, the association state of the Photobacterium leiognathi (PISOD) and Salmonella typhimurium (StSOD) enzymes, which differ in 11 out of 19 interface residues, was investigated by analytical ultracentrifugation. The same linkage pattern correlates quaternary assembly, active site metallation, and pH in the two enzymes albeit with quantitative differences. Both holo-enzymes are stable dimers at pH 6.8 and 8.0, although their shape is altered at alkaline pH. In contrast, dimer stability is affected differently by metal removal. Thus, apo-StSOD is a stable dimer at pH 6.8 whereas apo-PISOD is in reversible monomer-dimer equilibrium. In both apoproteins a pH increase to 8.0 favors monomerization. These effects prove the existence of long-range communication between the active site and the subunit interface and provide a structural explanation for the known functional differences between the two enzymes. (c) 2007 Elsevier Inc. All rights reserved.

Catacchio, B., D'Orazio, M., Battistoni, A., Chiancone, E. (2008). The dimeric assembly of Photobacterium leiognathi and Salmonella typhimurium SodC1 Cu,Zn superoxide dismutases is affected differently by active site demetallation and pH: An analytical ultracentrifuge study. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 471(1), 77-84 [10.1016/j.abb.2007.12.010].

The dimeric assembly of Photobacterium leiognathi and Salmonella typhimurium SodC1 Cu,Zn superoxide dismutases is affected differently by active site demetallation and pH: An analytical ultracentrifuge study

D'ORAZIO, MELANIA;BATTISTONI, ANDREA;
2008-01-01

Abstract

To establish whether the species-specific variations at the subunit interface of bacterial Cu,Zn superoxide dismutases affect dimer assembly, the association state of the Photobacterium leiognathi (PISOD) and Salmonella typhimurium (StSOD) enzymes, which differ in 11 out of 19 interface residues, was investigated by analytical ultracentrifugation. The same linkage pattern correlates quaternary assembly, active site metallation, and pH in the two enzymes albeit with quantitative differences. Both holo-enzymes are stable dimers at pH 6.8 and 8.0, although their shape is altered at alkaline pH. In contrast, dimer stability is affected differently by metal removal. Thus, apo-StSOD is a stable dimer at pH 6.8 whereas apo-PISOD is in reversible monomer-dimer equilibrium. In both apoproteins a pH increase to 8.0 favors monomerization. These effects prove the existence of long-range communication between the active site and the subunit interface and provide a structural explanation for the known functional differences between the two enzymes. (c) 2007 Elsevier Inc. All rights reserved.
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Rilevanza internazionale
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Sì, ma tipo non specificato
Settore BIO/10
English
Con Impact Factor ISI
Bacterial Cu,Zn superoxide dismutase; Long-range communication; Metal occupancy; Quaternary structure
Catacchio, B., D'Orazio, M., Battistoni, A., Chiancone, E. (2008). The dimeric assembly of Photobacterium leiognathi and Salmonella typhimurium SodC1 Cu,Zn superoxide dismutases is affected differently by active site demetallation and pH: An analytical ultracentrifuge study. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 471(1), 77-84 [10.1016/j.abb.2007.12.010].
Catacchio, B; D'Orazio, M; Battistoni, A; Chiancone, E
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/29108
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