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The multiple alternative oxidase proteins of soybean

Tanudji, M.; Djajanegara, I.; Daley, D.; McCabe, T.; Finnegan, Patrick M.; Day, David A.; Whelan, James M.

Description

The identity of the multiple alternative oxidase bands detected in various soybean tissues was investigated to determine if any modification that can alter the mobility on SDS-PAGE of the alternative oxidase occurs after mitochondrial import other than removal of the presequence. Comparison of the mature, in vitro imported products of AOX1, AOX2 and AOX3 in soybean cotyledons and rat liver mitechondria indicated that they had an identical apparent molecular mass to their in vitro expressed...[Show more]

dc.contributor.authorTanudji, M.
dc.contributor.authorDjajanegara, I.
dc.contributor.authorDaley, D.
dc.contributor.authorMcCabe, T.
dc.contributor.authorFinnegan, Patrick M.
dc.contributor.authorDay, David A.
dc.contributor.authorWhelan, James M.
dc.date.accessioned2015-12-13T23:24:11Z
dc.date.available2015-12-13T23:24:11Z
dc.identifier.issn0310-7841
dc.identifier.urihttp://hdl.handle.net/1885/92107
dc.description.abstractThe identity of the multiple alternative oxidase bands detected in various soybean tissues was investigated to determine if any modification that can alter the mobility on SDS-PAGE of the alternative oxidase occurs after mitochondrial import other than removal of the presequence. Comparison of the mature, in vitro imported products of AOX1, AOX2 and AOX3 in soybean cotyledons and rat liver mitechondria indicated that they had an identical apparent molecular mass to their in vitro expressed mature forms. This suggests that no modification specific to plant alternative oxidase altering the mobility on SDS-PAGE, took place. Changing the -2 and/or -3 Arg residue resulted in the inhibition of the generation of this mature form, suggesting that processing was most likely by the general mitochondrial processing peptidase. Comparison of the in vitro expressed mature forms to that detected by immunoblots of soybean tissues, required the induction of AOX1. Treatment of soybean cultured cells with antimycin A resulted in the induction of an additional band cross-reacting to monoclonal antibodies against the alternative oxidase. Comparison of the in vitro expressed mature forms to the alternative oxidase detected by western blotting indicated that they were identical in apparent molecular mass. These results indicated that no modification other than presequence removal, which alters mobility on SDS-PAGE, was required to generate the mature functional alternative oxidase proteins.
dc.publisherCSLI Publications
dc.sourceAustralian Journal of Plant Physiology
dc.subjectAlternative oxidase
dc.subjectAntimycin A
dc.subjectMitochondrial import
dc.subjectPrecursor processing
dc.subjectProtein modification
dc.subjectSoybean
dc.titleThe multiple alternative oxidase proteins of soybean
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume26
dc.date.issued1999
local.identifier.absfor060503 - Microbial Genetics
local.identifier.ariespublicationMigratedxPub23086
local.type.statusPublished Version
local.contributor.affiliationTanudji, M, University of Western Australia
local.contributor.affiliationDjajanegara, I, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationDaley, D, University of Western Australia
local.contributor.affiliationMcCabe, T, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationFinnegan, Patrick M, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationDay, David A, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationWhelan, James M, University of Western Australia
local.description.embargo2099-12-31
local.bibliographicCitation.startpage337
local.bibliographicCitation.lastpage344
local.identifier.doi10.1071/PP98122
dc.date.updated2015-12-12T09:19:31Z
local.identifier.scopusID2-s2.0-0032779980
CollectionsANU Research Publications

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