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Science 2 August 2002: Vol. 297. no. 5582, pp. 793 - 797 DOI: 10.1126/science.1072831
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Review
Plant Development: Regulation by Protein Degradation
Hanjo Hellmann,*
Mark Estelle
Many aspects of eukaryotic development depend on regulated
protein degradation by the ubiquitin-proteasome pathway. This highly conserved pathway promotes covalent attachment of ubiquitin to protein
substrates through the sequential action of three enzymes called a
ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2),
and a ubiquitin-protein ligase (E3). Most ubiquitinated proteins are
then targeted for degradation by the 26S proteasome. Recent
studies have also shown that the ubiquitin-related protein RUB/Nedd8
and the proteasome-related COP9 signalosome complex cooperate with the
ubiquitin-proteasome pathway to promote protein degradation. Most of
these components are conserved in all three eukaryotic kingdoms.
However, the known targets of the pathway in plants, and the
developmental processes they regulate, are specific to the plant
kingdom.
Molecular Cell and Developmental Biology, University of Texas,
Austin, TX 78712, USA.
*
Present address: Institut für Angewandte Genetik,
Molekulare Entwicklungsbiologie der Pflanzen, Albrecht-Thaer Weg 7, 14195 Berlin, Germany.
Present address: Myers Hall, Indiana University, 915 East
Third Street, Bloomington, IN 47405, USA.
To whom correspondence should be addressed. E-mail:
mestelle{at}bio.indiana.edu
Read the Full Text
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