A chloroplast envelope membrane protein containing a putative LrgB domain related to the control of bacterial death and lysis is required for chloroplast development in Arabidopsis thaliana

© 2011 The Authors. New Phytologist © 2011 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 193(2012), 1 vom: 01. Jan., Seite 81-95
1. Verfasser: Yang, Yanjun (VerfasserIn)
Weitere Verfasser: Jin, Haiyan, Chen, Yong, Lin, Weiqiang, Wang, Chaoqun, Chen, Zhehao, Han, Ning, Bian, Hongwu, Zhu, Muyuan, Wang, Junhui
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins Chloroplast Proteins DNA, Bacterial LrgB protein, Arabidopsis Membrane Proteins Phosphates T-DNA Nystatin mehr... 1400-61-9 Sucrose 57-50-1 Starch 9005-25-8
Beschreibung
Zusammenfassung:© 2011 The Authors. New Phytologist © 2011 New Phytologist Trust.
• A protein encoded by At1g32080 was consistently identified in proteomic studies of Arabidopsis chloroplast envelope membranes, but its function remained unclear. The protein, designated AtLrgB, may have evolved from a gene fusion of lrgA and lrgB. In bacteria, two homologous operons, lrgAB and cidAB, participate in an emerging mechanism to control cell death and lysis. • We aim to characterize AtLrgB using reverse genetics and cell biological and biochemical analysis. • AtLrgB is expressed in leaves, but not in roots. T-DNA insertion mutation of AtLrgB produced plants with interveinal chlorotic and premature necrotic leaves. Overexpression of full-length AtLrgB (or its LrgA and LrgB domains, separately), under the control of CaMV 35S promoter, produced plants exhibiting veinal chlorosis and delayed greening. At the end of light period, the T-DNA mutant had high starch and low sucrose contents in leaves, while the 35S:AtLrgB plants had low starch and high sucrose contents. Metabolite profiling revealed that AtLrgB appeared not to directly transport triose phosphate or hexose phosphates. In yeast cells, AtLrgB could augment nystatin-induced membrane permeability. • Our work indicates that AtLrgB is a new player in chloroplast development, carbon partitioning and leaf senescence, although its molecular mechanism remains to be established
Beschreibung:Date Completed 02.04.2012
Date Revised 20.04.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/j.1469-8137.2011.03867.x