An Arabidopsis indole-3-butyric acid-response mutant defective in PEROXIN6, an apparent ATPase implicated in peroxisomal function

Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1786-91. doi: 10.1073/pnas.0304368101. Epub 2004 Jan 26.

Abstract

Genetic evidence suggests that plant peroxisomes are the site of fatty acid beta-oxidation and conversion of the endogenous auxin indole-3-butyric acid (IBA) to the active hormone indole-3-acetic acid. Arabidopsis mutants that are IBA resistant and sucrose dependent during early development are likely to have defects in beta-oxidation of both IBA and fatty acids. Several of these mutants have lesions in peroxisomal protein genes. Here, we describe the Arabidopsis pex6 mutant, which is resistant to the inhibitory effects of IBA on root elongation and the stimulatory effects of IBA on lateral root formation. pex6 also is sucrose dependent during early seedling development and smaller and more pale green than WT throughout development. PEX6 encodes an apparent ATPase similar to yeast and human proteins required for peroxisomal biogenesis, and a human PEX6 cDNA can rescue the Arabidopsis pex6 mutant. The pex6 mutant has reduced levels of the peroxisomal matrix protein receptor PEX5, and pex6 defects can be partially rescued by PEX5 overexpression. These results suggest that PEX6 may facilitate PEX5 recycling and thereby promote peroxisomal matrix protein import.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Arabidopsis / metabolism*
  • Arabidopsis / ultrastructure
  • Arabidopsis Proteins*
  • Base Sequence
  • DNA Primers
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peroxisomes / physiology*
  • Sequence Homology, Amino Acid

Substances

  • Arabidopsis Proteins
  • DNA Primers
  • Adenosine Triphosphatases
  • ATPases Associated with Diverse Cellular Activities
  • PEROXIN6 protein, Arabidopsis
  • PEX6 protein, human
  • Pex6 protein, rat

Associated data

  • GENBANK/AY333116