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

Pollmann, Stephan and Neu, Daniel and Lehmann, Thomas and Berkowitz, Oliver and Schäfer, Tina and Weiler, Elmar W. (2006). Subcellular localization and tissue specific expression of amidase 1 from Arabidopsis thaliana. "Planta", v. 224 (n. 6); pp. 1241-1253. ISSN 0032-0935. https://doi.org/10.1007/s00425-006-0304-2.

Description

Title: Subcellular localization and tissue specific expression of amidase 1 from Arabidopsis thaliana
Author/s:
  • Pollmann, Stephan
  • Neu, Daniel
  • Lehmann, Thomas
  • Berkowitz, Oliver
  • Schäfer, Tina
  • Weiler, Elmar W.
Item Type: Article
Título de Revista/Publicación: Planta
Date: 2006
ISSN: 0032-0935
Volume: 224
Subjects:
Freetext Keywords: Amidase Amidohydrolase Arabidopsis Brassicaceae Fatty acid amide hydrolase Indole-3-acetic acid Indole-3-acetamide N-acylethanolamine Oleamide
Faculty: Centro de Investigación en Biotecnología y Genómica de Plantas (CBGP) (UPM)
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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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.

More information

Item ID: 14057
DC Identifier: http://oa.upm.es/14057/
OAI Identifier: oai:oa.upm.es:14057
DOI: 10.1007/s00425-006-0304-2
Official URL: http://link.springer.com/article/10.1007%2Fs00425-006-0304-2
Deposited by: Memoria Investigacion
Deposited on: 20 Dec 2012 11:37
Last Modified: 27 Apr 2016 11:10
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