A novel short-root gene encodes a glucosamine-6-phosphate acetyltransferase required for maintaining normal root cell shape in rice

Plant Physiol. 2005 May;138(1):232-42. doi: 10.1104/pp.104.058248. Epub 2005 Apr 22.

Abstract

Glycosylation is a posttranslational modification occurring in many secreted and membrane-associated proteins in eukaryotes. It plays important roles in both physiological and pathological processes. Most of these protein modifications depend on UDP-N-acetylglucosamine. In this study, a T-DNA insertional rice (Oryza sativa) mutant exhibiting a temperature-sensitive defect in root elongation was isolated. Genetic and molecular analysis indicated that the mutated phenotype was caused by loss of function of a gene encoding a glucosamine-6-P acetyltransferase (designated OsGNA1), which is involved in de novo UDP-N-acetylglucosamine biosynthesis. The aberrant root morphology of the gna1 mutant includes shortening of roots, disruption of microtubules, and shrinkage of cells in the root elongation zone. Our observations support the idea that protein glycosylation plays a key role in cell metabolism, microtubule stabilization, and cell shape in rice roots.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / chemistry
  • Acetyltransferases / genetics*
  • Amino Acid Sequence
  • Cell Shape
  • Cloning, Molecular
  • Consensus Sequence
  • Glucosamine 6-Phosphate N-Acetyltransferase
  • Kinetics
  • Molecular Sequence Data
  • Oryza / cytology
  • Oryza / genetics*
  • Phenotype
  • Plant Roots / cytology*
  • Plant Roots / enzymology
  • Restriction Mapping
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Acetyltransferases
  • Glucosamine 6-Phosphate N-Acetyltransferase

Associated data

  • GENBANK/AY722189