Plant Molecular Biology

, Volume 31, Issue 3, pp 693–699

Cloning of a cDNA for a chitinase homologue which lacks chitin-binding sites and is down-regulated by water stress and wounding

  • Shujung Chang
  • Jeff Puryear
  • Edward A. Funkhouser
  • Ronald J. Newton
  • John Cairney
Short Communication

DOI: 10.1007/BF00042242

Cite this article as:
Chang, S., Puryear, J., Funkhouser, E.A. et al. Plant Mol Biol (1996) 31: 693. doi:10.1007/BF00042242

Abstract

A cDNA clone (pLP6) of a gene which is repressed under water deficit was isolated from a loblolly pine (Pinus taeda L.) cDNA library and characterized. The predicted polypeptide encoded by pLP6 bears strong resemblance to a number of Class I chitinases. Howerver, LP6 lacks most of the amino-terminal and, consequently the signal peptide, cysteine-rich chitin-binding domain and glycine/proline-rich ‘hinge’ region, diagnostic of Class I chitinases, are absent. Although the cDNA is similar in size to its mRNA, the long open reading frame encoding the LP6 protein commences halfway through the mRNA, implying a 5′-untranslated region of over 700 nucleotides. Subfragments from the 5′ end of pLP6 hybridize to the same mRNA as do probes consisting of the entire cDNA. Reverse transcription (RT)-PCR experiments confirm that the cDNA derives from a single mRNA molecule. Analysis of the 5′-UTR revealed six upstream open reading frames and four inverted repeat structures. Expression of the pLP6 gene is repressed by water deficit stress and wounding. Possible functions and origin of this gene are discussed.

Key words

stress-responsive genes chitinase 5′-untranslated region loblolly pine 

Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Shujung Chang
    • 1
  • Jeff Puryear
    • 2
  • Edward A. Funkhouser
    • 3
  • Ronald J. Newton
    • 2
  • John Cairney
    • 1
  1. 1.Forest Biology GroupInstitute of Paper Science and TechnologyAtlantaUSA
  2. 2.Department of Forest ScienceTexas A&M UniversityCollege StationUSA
  3. 3.Department of BiochemistryTexas A&M UniversityCollege StationUSA

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