Abstract
The light harvesting like protein 3 (LIL 3) from higher plants, has been linked to functions in chlorophyll and tocopherol biosynthesis, photo-protection and chlorophyll transfer. However, the binding of chlorophyll to LIL3 is unclear. We present a reconstitution protocol for chlorophyll binding to LIL3 in DDM micelles. It is shown in the absence of lipids and carotenoids that reconstitution of chlorophyll binding to in vitro expressed LIL3 requires pre-incubation of reaction partners at room temperature. We show chlorophyll a but not chlorophyll b binding to LIL3 at a molar ratio of 1:1. Neither dynamic light scattering nor native PAGE, enabled a discrimination between binding of chlorophyll a and/or b to LIL3.
Highlights
The light harvesting like membrane protein 3 (LIL3) is a member of the light-harvesting complex protein family (LHCP) and characterized by the presence of a common LHC sequence motif [1]
The interaction of Chl with expressed and purified LIL3 was investigated in dodecylmaltoside (DDM) micelles using a process in which a temperature gradient induces a mass transport
Thermophoresis of molecules along a microscale temperature gradient is affected by molecular changes like size, charge or hydration shell, and a fluorescent reporter can be used to quantify a molecular interaction [20]
Summary
The light harvesting like membrane protein 3 (LIL3) is a member of the light-harvesting complex protein family (LHCP) and characterized by the presence of a common LHC sequence motif [1]. LIL3 is classified in the group of two-helix stress enhanced proteins (SEPs). Common ancestors of SEPs are the high-light inducible proteins (HLIP) in cyanobacteria, and the one-helix proteins (OHP) in plants [2]. LHCP genes harbor two LHC motifs which are associated with Chlorophyll (Chl) binding [1, 3, 4]. Proteins that harbor only one LHC motif, like LIL3, were determined to bind Chl. Microscale thermophoresis studies indicated that dimerization could provide the functional compensation for the missing LHC motif [5]
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