Up-regulation of a cysteine protease accompanies the ethylene-insensitive senescence of daylily (Hemerocallis) flowers

Plant Mol Biol. 1995 Jun;28(3):575-82. doi: 10.1007/BF00020403.


The flowers of daylily (Hemerocallis x hybrida cv. Cradle Song) open at midnight, start to senesce 12 h later, and are completely senescent by the following midnight. Differential screening of a cDNA library constructed from tepals of flowers showing incipient senescence revealed 25 clones that were strongly up-regulated in senescent tepals. Re-screening and interactive Southern analysis of these clones revealed 3 families of up-regulated clones. Transcripts of one clone, SEN10, were not detectable at midnight, but increased dramatically as senescence proceeded. The derived amino acid sequence of the full-length cDNA (SEN102) has strong homology with cysteine proteases that have been reported from other plant tissues. The sequence contains a secretory signal peptide and a probable prosequence upstream of the mature protein. Amino acids critical to the active site and structure of cysteine proteases are conserved, and the C-terminus of the polypeptide has a unique putative endoplasmic reticulum retention signal -RDEL.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism*
  • DNA, Complementary
  • DNA, Plant / genetics
  • Ethylenes / pharmacology*
  • Molecular Sequence Data
  • Plant Proteins*
  • Plants / drug effects
  • Plants / enzymology*
  • Plants / genetics
  • Sequence Homology, Amino Acid
  • Time Factors
  • Up-Regulation*


  • DNA, Complementary
  • DNA, Plant
  • Ethylenes
  • Plant Proteins
  • ethylene
  • Cysteine Endopeptidases
  • SEN102 protein, Hemerocallis

Associated data

  • GENBANK/X74406