Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions.

Fibrillins (FBNs) are plastidial proteins found in photosynthetic organisms from cyanobacteria to higher plants. The function of most FBNs remains unknown. Here, we focused on members of the FBN subgroup comprising FBN1a, FBN1b, and FBN2.

Interplay Between the N-Terminal Domains of Starch Synthase 3 Determines the Interaction of the Enzyme With the Starch Granule.

The elongation of the linear chains of starch is undertaken by starch synthases. class 3 of starch synthase (SS3) has a specific feature: a long N-terminal region containing starch binding domains (SBDs). In this work, we analyze the contribution of these domains to the localization pattern of the enzyme.

Thioredoxins m are major players in the multifaceted light-adaptive response in Arabidopsis thaliana.

Thioredoxins (TRXs) are well-known redox signalling players, which carry out post-translational modifications in target proteins. Chloroplast TRXs are divided into different types and have central roles in light energy uptake and the regulation of primary metabolism. The isoforms TRX m1, m2, and m4 from Arabidopsis thaliana are considered functionally related.

Starch granule initiation in Arabidopsis thaliana chloroplasts.

The initiation of starch granule formation and the mechanism controlling the number of granules per plastid have been some of the most elusive aspects of starch metabolism. This review covers the advances made in the study of these processes. The analyses presented herein depict a scenario in which starch synthase isoform 4 (SS4) provides the elongating activity necessary for the initiation of starch granule formation.