E. Mazzucotelli, S. Belloni, D. Marone, A. M. De Leonardis, D. Guerra, N. Di Fonzo, L. Cattivelli and A. M. Mastrangelo Pages 509 - 522 ( 14 )
The regulation of protein expression and activity has been for long time considered only in terms of transcription/ translation efficiency. In the last years, the discovery of post-transcriptional and post-translational regulation mechanisms pointed out that the key factor in determining transcript/protein amount is the synthesis/degradation ratio, together with post-translational modifications of proteins. Polyubiquitinaytion marks target proteins directed to degradation mediated by 26S-proteasome. Recent functional genomics studies pointed out that about 5% of Arabidopsis genome codes for proteins of ubiquitination pathway. The most of them (more than one thousand genes) correspond to E3 ubiquitin ligases that specifically recognise target proteins. The huge size of this gene family, whose members are involved in regulation of a number of biological processes including hormonal control of vegetative growth, plant reproduction, light response, biotic and abiotic stress tolerance and DNA repair, indicates a major role for protein degradation in control of plant life.
E3 ubiquitin ligase, post-translational regulation, plant
C.R.A.-Experimental Institute for Cereal Research, Section of Foggia, S.S. 16 km 675, 71100 Foggia,Italy.