Defective Kernel 1 (DEK1) is required for three-dimensional growth in Physcomitrella patens

© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 203(2014), 3 vom: 05. Aug., Seite 794-804
1. Verfasser: Perroud, Pierre-François (VerfasserIn)
Weitere Verfasser: Demko, Viktor, Johansen, Wenche, Wilson, Robert C, Olsen, Odd-Arne, Quatrano, Ralph S
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't DEK1 Physcomitrella patens cell division meristem plant morphogenesis three-dimensional development DNA, Complementary Plant Proteins
Beschreibung
Zusammenfassung:© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.
Orientation of cell division is critical for plant morphogenesis. This is evident in the formation and function of meristems and for morphogenetic transitions. Mosses undergo such transitions: from two-dimensional tip-growing filaments (protonema) to the generation of three-dimensional leaf-like structures (gametophores). The Defective Kernel 1 (DEK1) protein plays a key role in the perception of and/or response to positional cues that specify the formation and function of the epidermal layer in developing seeds of flowering plants. The moss Physcomitrella patens contains the highly conserved DEK1 gene. Using efficient gene targeting, we generated a precise PpDEK1 deletion (∆dek1), which resulted in normal filamentous growth of protonema. Two distinct mutant phenotypes were observed: an excess of buds on the protonema, and abnormal cell divisions in the emerging buds resulting in developmental arrest and the absence of three-dimensional growth. Overexpression of a complete PpDEK1 cDNA, or the calpain domain of PpDEK1 alone, successfully complements both phenotypes. These results in P. patens demonstrate the morphogenetic importance of the DEK1 protein in the control of oriented cell divisions. As it is not for protonema, it will allow dissection of the structure/function relationships of the different domains of DEK1 using gene targeting in null mutant background
Beschreibung:Date Completed 30.03.2015
Date Revised 21.10.2021
published: Print-Electronic
GENBANK: AAL38187
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.12844