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https://hdl.handle.net/2440/114079
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dc.contributor.author | Woodcock, J. | - |
dc.contributor.author | Goodwin, K. | - |
dc.contributor.author | Sandow, J. | - |
dc.contributor.author | Coolen, C. | - |
dc.contributor.author | Perugini, M. | - |
dc.contributor.author | Webb, A. | - |
dc.contributor.author | Pitson, S. | - |
dc.contributor.author | Lopez, A. | - |
dc.contributor.author | Carver, J. | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2018; 293(1):89-99 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/114079 | - |
dc.description.abstract | The 14-3-3 family of intracellular proteins are dimeric, multi-functional adaptor proteins that bind to and regulate the activities of many important signaling proteins. The subunits within 14-3-3 dimers are predicted to be stabilized by salt bridges that are largely conserved across the 14-3-3 protein family and allow the different isoforms to form heterodimers. Here, we have examined the contributions of conserved salt-bridging residues in stabilizing the dimeric state of 14-3-3ζ. Using analytical ultracentrifugation, our results revealed that Asp-21 and Glu-89 both play key roles in dimer dynamics and contribute to dimer stability. Furthermore, hydrogen-deuterium exchange coupled with mass spectrometry showed that mutation of Asp-21 promoted disorder in the amino-terminal helices of 14-3-3ζ, suggesting that this residue plays an important role in maintaining structure across the dimer interface. Intriguingly, a D21N 14-3-3ζ mutant exhibited enhanced molecular chaperone ability that prevented amorphous protein aggregation, suggesting a potential role for N-terminal disorder in 14-3-3ζ's poorly understood chaperone action. Taken together, these results imply that disorder in the N-terminal helices of 14-3-3ζ is a consequence of the dimer monomer dynamics and may play a role in conferring chaperone function to 14-3-3ζ protein. | - |
dc.description.statementofresponsibility | Joanna M. Woodcock, Katy L. Goodwin, Jarrod J. Sandow, Carl Coolen, Matthew A. Perugini, Andrew I. Webb, Stuart M. Pitson, Angel F. Lopez and John A. Carver | - |
dc.language.iso | en | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.rights | © 2018 by The American Society for Biochemistry and Molecular Biology, Inc. | - |
dc.source.uri | http://dx.doi.org/10.1074/jbc.m117.801019 | - |
dc.subject | 14-3-3 protein | - |
dc.subject | analytical ultracentrifugation | - |
dc.subject | dimer interface | - |
dc.subject | dimerization | - |
dc.subject | hydrogen-deuterium exchange | - |
dc.subject | molecular chaperone | - |
dc.subject | protein conformation | - |
dc.subject | protein disorder | - |
dc.subject | salt bridge | - |
dc.title | Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity | - |
dc.title.alternative | Role of salt bridges in the dimer interface of 14-3-3zeta in dimer dynamics, N-terminal alpha-helical order, and molecular chaperone activity | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1074/jbc.M117.801019 | - |
dc.relation.grant | http://purl.org/au-research/grants/nhmrc/1068087 | - |
dc.relation.grant | http://purl.org/au-research/grants/nhmrc/1042589 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Pitson, S. [0000-0002-9527-2740] | - |
dc.identifier.orcid | Lopez, A. [0000-0001-7430-0135] | - |
Appears in Collections: | Aurora harvest 3 Chemistry publications |
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