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PMID: 16738862 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Planta ·Vol. 224 ·No. 6 ·2006-11-00 ·Pages 1241-53

Pollmann S, Neu D, Lehmann T, Berkowitz O, Schäfer T, Weiler EW

Abstract

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 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.

MeSH Terms
Amidohydrolases/chemistry,metabolism Amino Acid Sequence Arabidopsis/enzymology Base Sequence Cloning, Molecular DNA Primers Molecular Sequence Data Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Subcellular Fractions/enzymology Substrate Specificity
Chemicals
DNA Primers Amidohydrolases amidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Pollmann Stephan
Department of Plant Physiology, Ruhr-University Bochum, Universitaetsstrasse 150, ND 2/27, 44801 Bochum, Germany. stephan.pollman@rub.de
Neu Daniel
Lehmann Thomas
Berkowitz Oliver
Schäfer Tina
Weiler Elmar W
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Article Info
Journal
Planta
Abbr.
Planta
ISSN
0032-0935
DOI
10.1007/s00425-006-0304-2
Email
stephan.pollman@rub.de
Published
2006-11-00
Pages
1241-53
Language
English
Region
Germany
NLM ID
1250576
Subset
IM
External Links
PubMed source DOI: 10.1007/s00425-006-0304-2 View journal details
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