The N-terminal domains of Bacillus subtilis CopA do not form a stable complex in the absence of their inter-domain linker

Zhou, Liang, Kay, Kristine L., Hecht, Oliver, Moore, Geoffrey R. and Le Brun, Nick E. ORCID: (2018) The N-terminal domains of Bacillus subtilis CopA do not form a stable complex in the absence of their inter-domain linker. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 1866 (2). pp. 275-282.

[thumbnail of Accepted manuscript] PDF (Accepted manuscript) - Accepted Version
Restricted to Repository staff only until 31 December 2099.

Request a copy
[thumbnail of Accepted manuscript]
PDF (Accepted manuscript) - Accepted Version
Available under License Creative Commons Attribution Non-commercial No Derivatives.

Download (1MB) | Preview


Copper-transporting P-type ATPases, which play important roles in trafficking Cu(I) across membranes for the biogenesis of copper proteins or for copper detoxification, contain a variable number of soluble metal-binding domains at their N-termini. It is increasingly apparent that these play an important role in regulating copper transport in a Cu(I)-responsive manner, but how they do this is unknown. CopA, a Cu(I)-transporter from Bacillus subtilis, contains two N-terminal soluble domains that are closely packed, with inter-domain interactions at two principal regions. Here, we sought to determine the extent to which the domains interact in the absence of their inter-domain covalent linker, and how their Cu(I)-binding properties are affected. Studies of a 1:1 mixture of separate CopAa and CopAb domains showed that the domains do not form a stable complex, with only indirect evidence of a weak interaction between them. Their Cu(I)-binding behaviour was distinct from that of the two domain protein and consistent with a lack of interaction between the domains. Cu(I)-mediated protein association was observed, but this occurred only between domains of the same type. Thus, the inter-domain covalent link between CopAa and CopAb is essential for inter-domain interactions and for Cu(I)-binding behaviour.

Item Type: Article
Uncontrolled Keywords: copper trafficking,metallochaperones,homeostasis,metal transport
Faculty \ School: Faculty of Science > School of Chemistry
UEA Research Groups: Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Chemistry of Life Processes
Depositing User: Pure Connector
Date Deposited: 15 Nov 2017 06:07
Last Modified: 21 Oct 2022 17:30
DOI: 10.1016/j.bbapap.2017.11.008

Actions (login required)

View Item View Item