Molecular cloning and characterization of an arginine decarboxylase gene up-regulated by chilling stress in rice seedlings

J Plant Physiol. 2007 May;164(5):645-54. doi: 10.1016/j.jplph.2006.04.006.

Abstract

We cloned a rice cDNA encoding a putative arginine decarboxylase (ADC) protein, a key enzyme involved with putrescine (Put) biosynthesis in plants. The isolated full-length cDNA (OsADC1) contains an insert consisting of 2451 bp. The longest open reading frame within encodes a putative protein of 702 amino acids, with a calculated molecular mass of 74 kDa and an isoelectric point of 4.9. ClustalW alignment revealed that the deduced OsADC1 protein sequence shares overall 60% and 61% identity at the amino acid level with the Pisum sativum and Glycine max ADC proteins, respectively. Additionally, several OsADC1 regions exhibited striking similarity with these two other plant ADC protein sequences, including motifs characteristic of ADC proteins. Further, RNA gel blot analysis revealed markedly increased OsADC1 mRNA levels in rice seedling leaves subjected to chilling stress. Interestingly, this treatment induced a concomitant increase in free Put levels in these samples, coincident with the observed elevated OsADC1 mRNA levels. To our knowledge, this represents the first direct evidence supporting essentially chilling-specific regulation of a rice ADC gene that also potentially influences Put accumulation, a phenomenon previously noted in cold-stressed rice seedlings.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carboxy-Lyases / chemistry
  • Carboxy-Lyases / genetics*
  • Carboxy-Lyases / metabolism*
  • Cloning, Molecular
  • Cold Temperature*
  • Enzyme Induction*
  • Gene Expression Regulation, Plant
  • Oryza / enzymology*
  • Oryza / genetics*
  • Phylogeny
  • Seedlings / enzymology
  • Seedlings / genetics
  • Up-Regulation*

Substances

  • Carboxy-Lyases
  • arginine decarboxylase