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Subcellular localization and tissue specific expression of amidase 1 from Arabidopsis thaliana

Pollmann, Stephan; Neu, Daniel; Lehmann, Thomas; Berkowitz, Oliver; Schafer, Tina; Weiler, Elmar W

Description

Amidase 1 (AMI1) from Arabidopsis thaliana converts indole-3-acetamide (IAM), into indole-3-acetic acid (IAA). AMI1 is part of a small isogene family comprising seven members in A. thaliana encoding proteins which share a conserved glycine- and serine-rich amidase-signature. One member of this family has been characterized as an N-acylethanolamine-cleaving fatty acid amidohydrolase (FAAH) and two other members are part of the preprotein translocon of the outer envelope of chloroplasts (Toc...[Show more]

dc.contributor.authorPollmann, Stephan
dc.contributor.authorNeu, Daniel
dc.contributor.authorLehmann, Thomas
dc.contributor.authorBerkowitz, Oliver
dc.contributor.authorSchafer, Tina
dc.contributor.authorWeiler, Elmar W
dc.date.accessioned2015-12-07T22:16:23Z
dc.identifier.issn0032-0935
dc.identifier.urihttp://hdl.handle.net/1885/18008
dc.description.abstractAmidase 1 (AMI1) from Arabidopsis thaliana converts indole-3-acetamide (IAM), into indole-3-acetic acid (IAA). AMI1 is part of a small isogene family comprising seven members in A. thaliana encoding proteins which share a conserved glycine- and serine-rich amidase-signature. One member of this family has been characterized as an N-acylethanolamine-cleaving fatty acid amidohydrolase (FAAH) and two other members are part of the preprotein translocon of the outer envelope of chloroplasts (Toc complex) or mitochondria (Tom complex) and presumably lack enzymatic activity. Among the hitherto characterized proteins of this family, AMI1 is the only member with indole-3-acetamide hydrolase activity, and IAM is the preferred substrate while N-acylethanolamines and oleamide are not hydrolyzed significantly, thus suggesting a role of AMI1 in auxin biosynthesis. Whereas the enzymatic function of AMI1 has been determined in vitro, the subcellular localization of the enzyme remained unclear. By using different GFP-fusion constructs and an A. thaliana transient expression system, we show a cytoplasmic localization of AMI1. In addition, RT-PCR and anti-amidase antisera were used to examine tissue specific expression of AMI1 at the transcriptional and translational level, respectively. AMI1-expression is strongest in places of highest IAA content in the plant. Thus, it is concluded that AMI1 may be involved in de novo IAA synthesis in A. thaliana.
dc.publisherSpringer
dc.sourcePlanta
dc.subjectKeywords: amidase; primer DNA; amino acid sequence; Arabidopsis; article; cell fractionation; chemistry; enzyme specificity; enzymology; metabolism; molecular cloning; molecular genetics; nucleotide sequence; reverse transcription polymerase chain reaction; sequenc Amidase; Amidohydrolase; Arabidopsis; Brassicaceae; Fatty acid amide hydrolase; Indole-3-acetamide; Indole-3-acetic acid; N-acylethanolamine; Oleamide
dc.titleSubcellular localization and tissue specific expression of amidase 1 from Arabidopsis thaliana
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume224
dc.date.issued2006
local.identifier.absfor060705 - Plant Physiology
local.identifier.ariespublicationu4070025xPUB3
local.type.statusPublished Version
local.contributor.affiliationPollmann, Stephan, Ruhr-University Bochum
local.contributor.affiliationNeu, Daniel, Ruhr-University Bochum
local.contributor.affiliationLehmann, Thomas, Ruhr-University Bochum
local.contributor.affiliationBerkowitz, Oliver, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationSchafer, Tina, Ruhr-University Bochum
local.contributor.affiliationWeiler, Elmar W, Ruhr-University Bochum
local.description.embargo2037-12-31
local.bibliographicCitation.issue6
local.bibliographicCitation.startpage1241
local.bibliographicCitation.lastpage53
local.identifier.doi10.1007/s00425-006-0304-2
dc.date.updated2015-12-07T07:50:46Z
local.identifier.scopusID2-s2.0-33751111975
CollectionsANU Research Publications

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