RT Journal Article
SR Electronic
T1 Ubiquitylation activates a peptidase that promotes cleavage and destabilization of its activating E3 ligases and diverse growth regulatory proteins to limit cell proliferation in Arabidopsis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 090563
DO 10.1101/090563
A1 Hui Dong
A1 Jack Dumenil
A1 Fu-Hao Lu
A1 Li Na
A1 Hannes Vanhaeren
A1 Christin Naumann
A1 Maria Klecker
A1 Rachel Prior
A1 Caroline Smith
A1 Neil McKenzie
A1 Gerhard Saalbach
A1 Liangliang Chen
A1 Tian Xia
A1 Nathalie Gonzalez
A1 Mathilde Seguela
A1 Dirk Inze
A1 Nico Dissmeyer
A1 Yunhai Li
A1 Michael W. Bevan
YR 2016
UL http://biorxiv.org/content/early/2016/11/30/090563.abstract
AB The characteristic shapes and sizes of organs are established by cell proliferation patterns and final cell sizes, but the underlying molecular mechanisms coordinating these are poorly understood. Here we characterize a ubiquitin-activated peptidase called DA1 that limits the duration of cell proliferation during organ growth in Arabidopsis thaliana. The peptidase is activated by two RING E3 ligases, BB and DA2, which are subsequently cleaved by the activated peptidase and destabilized. In the case of BB, cleavage leads to destabilization by the RING E3 ligase PRT1 of the N-end rule pathway. DA1 peptidase activity also cleaves the de-ubiquitylase UBP15, which promotes cell proliferation, and the transcription factors TCP15 and TCP22, which promote cell proliferation proliferation and repress endoreduplication. We propose that DA1 peptidase activity regulates the duration of cell proliferation and the transition to endoreduplication and differentiation during organ formation in plants by coordinating the destabilization of regulatory proteins.