Planta

, Volume 221, Issue 5, pp 619–636

Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana

  • Bonnie C. McCaig
  • Richard B. Meagher
  • Jeffrey F. D. Dean
Original Article

DOI: 10.1007/s00425-004-1472-6

Cite this article as:
McCaig, B.C., Meagher, R.B. & Dean, J.F.D. Planta (2005) 221: 619. doi:10.1007/s00425-004-1472-6

Abstract

Completed genome sequences have made it clear that multicopper oxidases related to laccase are widely distributed as multigene families in higher plants. Laccase-like multicopper oxidase (LMCO) sequences culled from GenBank and the Arabidopsis thaliana genome, as well as those from several newly cloned genes, were used to construct a gene phylogeny that clearly divided plant LMCOs into six distinct classes, at least three of which predate the evolutionary divergence of angiosperms and gymnosperms. Alignments of the predicted amino acid sequences highlighted regions of variable sequence flanked by the highly conserved copper-binding domains that characterize members of this enzyme family. All of the predicted proteins contained apparent signal sequences. The expression of 13 of the 17 LMCO genes in A. thaliana was assessed in different tissues at various stages of development using RT-PCR. A diversity of expression patterns was demonstrated with some genes being expressed in a constitutive fashion, while others were only expressed in specific tissues at a particular stage of development. Only a few of the LMCO genes were expressed in a pattern that could be considered consistent with a major role for these enzymes in lignin deposition. These results are discussed in the context of other potential physiological functions for plant LMCOs, such as iron metabolism and wound healing.

Keywords

Iron metabolism Laccase Lignification Phylogeny 

Abbreviations

BLAST

Basic local alignment search tool

CTAB

Cetyl trimethylammonium bromide

LMCO

Laccase-like multicopper oxidase

MCO

Multicopper oxidase

MPSS

Massively parallel signature sequencing

PCR

Polymerase chain reaction

pI

Isoelectric point

RACE

Rapid amplification of cDNA ends

RT-PCR

Reverse transcript polymerase chain reaction

TBE

Tris borate EDTA buffer

Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  • Bonnie C. McCaig
    • 1
    • 3
  • Richard B. Meagher
    • 2
  • Jeffrey F. D. Dean
    • 1
  1. 1.Daniel B. Warnell School of Forest ResourcesUniversity of GeorgiaAthensUSA
  2. 2.Department of GeneticsUniversity of GeorgiaAthensUSA
  3. 3.Department of Energy-Plant Research LaboratoryMichigan State UniversityEast LansingUSA

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