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 Dong, Hui
A1 Dumenil, Jack
A1 Lu, Fu-Hao
A1 Na, Li
A1 Vanhaeren, Hannes
A1 Naumann, Christin
A1 Klecker, Maria
A1 Prior, Rachel
A1 Smith, Caroline
A1 McKenzie, Neil
A1 Saalbach, Gerhard
A1 Chen, Liangliang
A1 Xia, Tian
A1 Gonzalez, Nathalie
A1 Seguela, Mathilde
A1 Inze, Dirk
A1 Dissmeyer, Nico
A1 Li, Yunhai
A1 Bevan, Michael W.
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.