Lil3 dimerization and chlorophyll binding in Arabidopsis thaliana
Mork-Jansson A, Gargano D, Kmiec K, Furnes C, Shevela D, Eichacker L
2015 vol: 589 (20) pp: 3064-3070
The two-helix light harvesting like (Lil) protein Lil3 belongs to the family of chlorophyll binding light harvesting proteins of photosynthetic membranes. A function in tetrapyrrol synthesis and stabilization of geranylgeraniol reductase has been shown. Lil proteins contain the chlorophyll a/b-binding motif; however, binding of chlorophyll has not been demonstrated. We find that Lil3.2 fromArabidopsis thaliana forms heterodimers with Lil3.1 and binds chlorophyll. Lil3.2 heterodimerization (25 ± 7.8 nM) is favored relative to homodimerization (431 ± 59 nM). Interaction of Lil3.2 with chlorophyll a (231 ± 49 nM) suggests that heterodimerization precedes binding of chlorophyll inArabidopsis thaliana.
Topics: Aromatic compounds, Complex samples, Dimerization & oligomerization, Lipids, Measure binding affinity, Membrane proteins, Monolith, Microscale Thermophoresis, Plant proteins, Proteins, Publications