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Characterization of 25 full-length <Emphasis Type="Italic">S-RNase</Emphasis> alleles,including flanking regions,from a pool of resequenced apple cultivars
Authors:Paolo De Franceschi  Luca Bianco  Alessandro Cestaro  Luca Dondini  Riccardo Velasco
Institution:1.The Center for Lignocellulose Structure and Formation,The Pennsylvania State University,University Park,USA;2.Department of Biochemistry and Molecular Biology,The Pennsylvania State University,University Park,USA;3.Department of Biology,The Pennsylvania State University,University Park,USA;4.Department of Horticulture,Michigan State University,East Lansing,USA;5.University Park,USA
Abstract:

Key message

Our work focuses on understanding the lifetime and thus stability of the three main cellulose synthase (CESA) proteins involved in primary cell wall synthesis of Arabidopsis. It had long been thought that a major means of CESA regulation was via their rapid degradation. However, our studies here have uncovered that AtCESA proteins are not rapidly degraded. Rather, they persist for an extended time in the plant cell.

Abstract

Plant cellulose is synthesized by membrane-embedded cellulose synthase complexes (CSCs). The CSC is composed of cellulose synthases (CESAs), of which three distinct isozymes form the primary cell wall CSC and another set of three isozymes form the secondary cell wall CSC. We determined the stability over time of primary cell wall (PCW) CESAs in Arabidopsis thaliana seedlings, using immunoblotting after inhibiting protein synthesis with cycloheximide treatment. Our work reveals very slow turnover for the Arabidopsis PCW CESAs in vivo. Additionally, we show that the stability of all three CESAs within the PCW CSC is altered by mutations in individual CESAs, elevated temperature, and light conditions. Together, these results suggest that CESA proteins are very stable in vivo, but that their lifetimes can be modulated by intrinsic and environmental cues.
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