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A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor

DOI: 10.1007/s00018-014-1658-4 DOI Help
PMID: 24915944 PMID Help

Authors: Matthew D. Hitchings (College of Medicine, Swansea University) , Philip Townsend (Department of Chemistry, School of Biological and Biomedical Sciences, University Science Laboratories, Durham University) , Ehmke Pohl (Department of Chemistry, School of Biological and Biomedical Sciences, University Science Laboratories, Durham University) , Paul D. Facey (College of Medicine, Swansea University) , D. Hugh Jones (College of Medicine, Swansea University) , Paul J. Dyson (College of Medicine, Swansea University) , Ricardo Del Sol (College of Medicine, Swansea University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cellular And Molecular Life Sciences

State: Published (Approved)
Published: June 2014
Diamond Proposal Number(s): 7864

Abstract: Dps proteins are members of an extensive family of proteins that oxidise and deposit iron in the form of ferric oxide, and are also able to bind DNA. Ferroxidation centres are formed at the interface of anti-parallel dimers, which further assemble into dodecameric nanocages with a hollow core where ferric oxide is deposited. Streptomyces coelicolor encodes three Dps-like proteins (DpsA, B and C). Despite sharing the conserved four-helix bundle organisation observed in members of the Dps family, they display significant differences in the length of terminal extensions, or tails. DpsA possess both N- and C-terminal tails of different lengths, and their removal affects quaternary structure assembly to varying degrees. DpsC quaternary structure, on the other hand, is heavily dependent on its N-terminal tail as its removal abolishes correct protein folding. Analysis of the crystal structure of dodecamers from both proteins revealed remarkable differences in the position of tails and interface surface area; and provides insight to explain the differences in biochemical behaviour observed while comparing DpsA and DpsC.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 26/09/2014 14:10

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