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JXB Advance Access originally published online on March 21, 2006
Journal of Experimental Botany 2006 57(6):1431-1443; doi:10.1093/jxb/erj123
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© The Author [2006]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. The online version of this article has been published under an Open Access model. Users are entitled to use, reproduce, disseminate, or display the Open Access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Society for Experimental Biology are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact: journals.permissions@oxfordjournals.org

RESEARCH PAPER

Two new cysteine proteinases with specific expression patterns in mature and senescent tobacco (Nicotiana tabacum L.) leaves*

Getu Beyene1, Christine H. Foyer2 and Karl J. Kunert1,{dagger}

1Forestry and Agricultural Biotechnology Institute, Botany Department, University of Pretoria, Hillcrest, Pretoria 0002, South Africa
2Crop Performance and Improvement Division, Rothamsted Research, Harpenden, Herts AL5 2JQ, UK

{dagger} To whom correspondence should be addressed. E-mail: karl.kunert{at}fabi.up.ac.za

Cysteine proteinases are involved in various physiological and developmental processes in plants. Two cDNAs from senescent and non-senescent tobacco leaves were isolated with degenerate primers designed from conserved regions of plant senescence-associated cysteine proteinases using rapid amplification of cDNA ends (RACE). Both sequences encode papain-like cysteine proteinases: the 833 bp fragment (NtCP1) encoding a C-terminus partial sequence of a putative tobacco cysteine proteinase gene whereas the 1300 bp fragment (NtCP2) is a full-length cysteine proteinase. On the amino acid sequence level, NtCP1 has a high similarity with other senescence-associated cysteine proteinases. It is expressed only in senescent leaves. It is not induced in mature green leaves upon exposure to drought or heat. These results suggest that it might be a good developmental senescence marker in tobacco. By contrast, NtCP2 has a high similarity to KDEL-tailed cysteine proteinases and is expressed in mature green leaves. Both drought and heat decreased NtCP2 transcript abundance in mature green leaves. It is concluded that NtCP1 is a senescence-specific cysteine proteinase whereas NtCP2 fulfils roles in green leaves that might be similar to those of KDEL-tailed cysteine proteinases involved, for example, in programmed cell death.

Key words: Cysteine proteinase, KDEL motif, senescence markers, tobacco


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