JXB Advance Access published online on April 3, 2009
Journal of Experimental Botany, doi:10.1093/jxb/erp076
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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RESEARCH PAPER |
Transcriptional activation of a 37 kDa ethylene responsive cysteine protease gene, RbCP1, is associated with protein degradation during petal abscission in rose



Plant Gene Expression Laboratory, National Botanical Research Institute, Lucknow-226001, India
To whom correspondence should be addressed: E-mail: saneanil{at}rediffmail.com
Cysteine proteases play an important role in several developmental processes in plants, particularly those related to senescence and cell death. A cysteine protease gene, RbCP1, has been identified that encodes a putative protein of 357 amino acids and is expressed in the abscission zone (AZ) of petals in rose. The gene was responsive to ethylene in petals, petal abscission zones, leaves, and thalamus. The expression of RbCP1 increased during both ethylene-induced as well as natural abscission and was inhibited by 1-MCP. Transcript accumulation of RbCP1 was accompanied by the appearance of a 37 kDa cysteine protease, a concomitant increase in protease activity and a substantial decrease in total protein content in the AZ of petals. Agro-injection of rose petals with a 2.0 kb region upstream of the RbCP1 gene could drive GUS expression in an abscission zone-specific manner and was blocked by 1-MCP. It is concluded that petal abscission is associated with a decrease in total protein content resulting from rapid transcription of RbCP1 and the expression of a 37 kDa protease.
Key words: Abscission, agro-infiltration, cysteine protease, ethylene, petal, programmed cell death, RbCP1, rose, senescence
* Present address: International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi -110067, India.
Both authors contributed equally to the paper.
Received 4 November 2008; Revised 15 February 2009 Accepted 23 February 2009