Glycinebetaine stabilizes the association of extrinsic proteins with the photosynthetic oxygen-evolving complex.
The photosynthetic oxygen-evolving activity of the photosystem 2 complex, prepared from spinach, was labile when the complex was exposed to high-salt conditions under which the extrinsic proteins were dissociated from the complex. Glycinebetaine prevented the dissociation of the 18-kDa and the 23-kDa extrinsic proteins from the photosystem 2 complex in the presence of 1 M NaCl. It also prevented the dissociation of the 33-kDa extrinsic protein from the complex in the presence of 1 M MgCl2 or 1 M CaCl2. The oxygen-evolving activity of the photosystem 2 complex was stabilized by glycinebetaine when the complex was subjected to treatment with NaCl and MgCl2.
Murata
N
N
Department of Regulation Biology, National Institute for Basic Biology, Okazaki, Japan.
Mohanty
P S
PS
Hayashi
H
H
Papageorgiou
G C
GC
D001622:Betaine / Q000494:pharmacology*; D002736:Chloroplasts / Q000737:chemistry*; D015636:Magnesium Chloride / Q000494:pharmacology; D008565:Membrane Proteins / Q000737:chemistry*; D010100:Oxygen / Q000378:metabolism; D010788:Photosynthesis / Q000187:drug effects; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000187:drug effects; D012965:Sodium Chloride / Q000494:pharmacology
D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D015636:Magnesium Chloride; D001622:Betaine; D012965:Sodium Chloride; D010100:Oxygen