Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains.

ABSTRACT: Cellulose synthase (CesA) proteins are components of CesA complexes (rosettes) and are thought to catalyze the chain elongation step in glucan polymerization. Little is understood about rosette assembly, including how CesAs interact with each other or with other components within the complexes. The first conserved region at the N terminus of plant CesA proteins contains two putative zinc fingers that show high homology to the RING-finger motif. We show that this domain in GhCesA1 can bind two atoms of Zn2+, as predicted by its structure. Analysis in the yeast two-hybrid system indicates that the N-terminal portions of cotton fiber GhCesA1 and GhCesA2 containing these domains can interact to form homo- or heterodimers. Although Zn(2+) binding occurs only when the protein is in the reduced f

SUBMITTER: Kurek I 

PROVIDER: S-EPMC123218 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature