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Functional characterisation of ganglioside-induced differentiation-associated protein 1 as a glutathione transferase

Shield, Alison; Murray, Tracy; Board, Philip

Description

Mutations in the ganglioside-induced differentiation-associated protein 1 (GDAP1) gene have been linked with Charcot-Marie-Tooth (CMT) disease. This protein, and its paralogue GDAP1L1, appear to be structurally related to the cytosolic glutathione S-transferases (GST) including an N-terminal thioredoxin fold domain with conserved active site residues. The specific function, of GDAP1 remains unknown. To further characterise their structure and function we purified recombinant human GDAP1 and...[Show more]

dc.contributor.authorShield, Alison
dc.contributor.authorMurray, Tracy
dc.contributor.authorBoard, Philip
dc.date.accessioned2015-12-13T23:03:55Z
dc.identifier.issn0006-291X
dc.identifier.urihttp://hdl.handle.net/1885/85136
dc.description.abstractMutations in the ganglioside-induced differentiation-associated protein 1 (GDAP1) gene have been linked with Charcot-Marie-Tooth (CMT) disease. This protein, and its paralogue GDAP1L1, appear to be structurally related to the cytosolic glutathione S-transferases (GST) including an N-terminal thioredoxin fold domain with conserved active site residues. The specific function, of GDAP1 remains unknown. To further characterise their structure and function we purified recombinant human GDAP1 and GDAP1L1 proteins using bacterial expression and immobilised metal affinity chromatography. Like other cytosolic GSTs, GDAP1 protein has a dimeric structure. Although the full-length proteins were largely insoluble, the deletion of a proposed C-terminal transmembrane domain allowed the preparation of soluble protein. The purified proteins were assayed for glutathione-dependent activity against a library of 'prototypic' GST substrates. No evidence of glutathione-dependent activity or an ability to bind glutathione immobilised on agarose was found.
dc.publisherAcademic Press
dc.sourceBiochemical and Biophysical Research Communications
dc.subjectKeywords: agarose; dimer; ganglioside induced diffentiation associated protein 1; ganglioside induced differentiation associated protein 1 like 1 protein; glutathione; glutathione transferase; metal; recombinant protein; unclassified drug; affinity chromatography; Charcot-Marie-Tooth disease; Ganglioside-induced differentiation-associated protein; Glutathione transferase; Mitochondria
dc.titleFunctional characterisation of ganglioside-induced differentiation-associated protein 1 as a glutathione transferase
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume347
dc.date.issued2006
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationMigratedxPub13377
local.type.statusPublished Version
local.contributor.affiliationShield, Alison, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationMurray, Tracy, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue4
local.bibliographicCitation.startpage859
local.bibliographicCitation.lastpage66
local.identifier.doi10.1016/j.bbrc.2006.06.189
dc.date.updated2015-12-12T07:52:16Z
local.identifier.scopusID2-s2.0-33746353696
CollectionsANU Research Publications

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