V. Valpuesta et al., UP-REGULATION OF A CYSTEINE PROTEASE ACCOMPANIES THE ETHYLENE-INSENSITIVE SENESCENCE OF DAYLILY (HEMEROCALLIS) FLOWERS, Plant molecular biology, 28(3), 1995, pp. 575-582
The flowers of daylily (Hemerocallis x hybrida cv. Cradle Song) open a
t midnight, start to senesce 12 h later, and are completely senescent
by the following midnight. Differential screening of a cDNA library co
nstructed from tepals of flowers showing incipient senescence revealed
25 clones that were strongly up-regulated in senescent tepals. Re-scr
eening and interactive Southern analysis of these clones revealed 3 fa
milies of up-regulated clones. Transcripts of one clone, SEN10, were n
ot detectable at midnight, but increased dramatically as senescence pr
oceeded. The derived amino acid sequence of the full-length cDNA (SEN1
02) has strong homology with cysteine proteases that have been reporte
d from other plant tissues. The sequence contains a secretory signal p
eptide and a probable prosequence upstream of the mature protein. Amin
o acids critical to the active site and structure of cysteine protease
s are conserved, and the C-terminus of the polypeptide has a unique pu
tative endoplasmic reticulum retention signal -RDEL.