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

Pollmann, Stephan; Neu, Daniel; Lehmann, Thomas; Berkowitz, Oliver; Schäfer, Tina y 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.

Descripción

Título: Subcellular localization and tissue specific expression of amidase 1 from Arabidopsis thaliana
Autor/es:
  • Pollmann, Stephan
  • Neu, Daniel
  • Lehmann, Thomas
  • Berkowitz, Oliver
  • Schäfer, Tina
  • Weiler, Elmar W.
Tipo de Documento: Artículo
Título de Revista/Publicación: Planta
Fecha: 2006
Volumen: 224
Materias:
Palabras Clave Informales: Amidase Amidohydrolase Arabidopsis Brassicaceae Fatty acid amide hydrolase Indole-3-acetic acid Indole-3-acetamide N-acylethanolamine Oleamide
Escuela: Centro de Investigación en Biotecnología y Genómica de Plantas (CBGP) (UPM)
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

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.

Más información

ID de Registro: 14057
Identificador DC: http://oa.upm.es/14057/
Identificador OAI: oai:oa.upm.es:14057
Identificador DOI: 10.1007/s00425-006-0304-2
URL Oficial: http://link.springer.com/article/10.1007%2Fs00425-006-0304-2
Depositado por: Memoria Investigacion
Depositado el: 20 Dic 2012 11:37
Ultima Modificación: 27 Abr 2016 11:10
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