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KORRIGAN1 interacts specifically with integral components of the cellulose synthase machinery.

Research paper by Nasim N Mansoori, Jaap J Timmers, Thierry T Desprez, Claire L CL Alvim-Kamei, Claire L A CL Kamei, Dianka C T DC Dees, Jean-Paul JP Vincken, Richard G F RG Visser, Herman H Höfte, Samantha S Vernhettes, Luisa M LM Trindade

Indexed on: 11 Nov '14Published on: 11 Nov '14Published in: PloS one



Abstract

Cellulose is synthesized by the so called rosette protein complex and the catalytic subunits of this complex are the cellulose synthases (CESAs). It is thought that the rosette complexes in the primary and secondary cell walls each contains at least three different non-redundant cellulose synthases. In addition to the CESA proteins, cellulose biosynthesis almost certainly requires the action of other proteins, although few have been identified and little is known about the biochemical role of those that have been identified. One of these proteins is KORRIGAN (KOR1). Mutant analysis of this protein in Arabidopsis thaliana showed altered cellulose content in both the primary and secondary cell wall. KOR1 is thought to be required for cellulose synthesis acting as a cellulase at the plasma membrane-cell wall interface. KOR1 has recently been shown to interact with the primary cellulose synthase rosette complex however direct interaction with that of the secondary cell wall has never been demonstrated. Using various methods, both in vitro and in planta, it was shown that KOR1 interacts specifically with only two of the secondary CESA proteins. The KOR1 protein domain(s) involved in the interaction with the CESA proteins were also identified by analyzing the interaction of truncated forms of KOR1 with CESA proteins. The KOR1 transmembrane domain has shown to be required for the interaction between KOR1 and the different CESAs, as well as for higher oligomer formation of KOR1.