Chloroplast Biogenesis - Assembly of Chlorophyll into Chlorophyll-binding Proteins
Peng Wang, Daniel Hey, Josephine Herbst, Maxi Rothbart, Andreas Richter
The view of free-floating proteins in the soluble or membranous phase of subcellular compartments has been replaced with a new concept based on the insights into the subcompartmental organization of metabolic pathways, including Chl biosynthesis. It is expected that the organellar topology of tetrapyrrole biosynthesis will include the formation of transient and stable complexes with specific sets of proteins. These multiprotein complexes provide a protected area of enriched, functionally and structurally interacting proteins, increase the accuracy of distinct biochemical reactions, enable substrate channeling, ensure the separation of disturbing and antagonistic pathways and prevent the release of toxic intermediates, which may cause photooxidative reactions. All in all, it is hypothesized that the high level of suborganellar organization enables a precise and adequate supply of endproducts to the sites of assembly with Chl-binding proteins of photosynthesis, but these processes are achieved by additional assembly and auxiliary factors and chaperones.
Light-harvesting-like 3 (LIL3) proteins in Arabidopsis
One-helix proteins (OHPs) in Arabidopsis
TPR proteins and their role in chloroplasts
Coordination between tetrapyrrole biosynthesis and chloroplast SRP pathway