Brookhaven National Laboratory
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Upton, NY 11973-5000
Molecular mechanisms protect higher plants and algae against cellular
damage during stress arising from excessive light collection by the
photosynthetic antenna. Earlier studies showed that reversible phosphorylations
of the light-harvesting protein complex of photosystem II (LHC-II) and the
photosystem II reaction centers are driven by two distinct protein kinases,
and regulate excitation energy distribution in low to moderate light
intensity regimes. At higher intensities typical of the photoinhibition
regime, LHC-II in thylakoid membranes and in detergent-isolated, two-dimensional
crystals undergoes profound reorganization evidenced by loss of chirality.
Scanning Transmission Electron Microscopy (STEM) analysis showed that hexagonal
crystalline arrays of LHC-II are disrupted into polydisperse particles under these
conditions, consistent with a proposed trimer-monomer transition in LHC-II.
STEM also revealed a novel microcrystalline form of lipid-depleted LHC-II which has
strong chirality but is structurally resistant to intense light. Its unit cell is
rhombic, and the two-dimensional crystals have uniquely high mean mass per unit area.
Current experiments explore the organization of trimers in these microcrystals.
Dunn J.J., McCorkle S.R., Praissman L.A., Hind G., van der Lelie D., Bahou W.F., Gnatenko D.V. and Krause M.K.
Genomic Signature Tags (GSTs): A system for profiling genomic DNA.
Genome Research, 12:1756-65 (2002).
Race H.L., Forsberg J., Hind G. and Allen J.F.
Photosystem II-associated protein kinase phosphorylates a novel 6.3 kDa
protein which subsequently dissociates from photosystem II core complexes.
In: Photosynthesis: Mechanisms and Effects, Proceedings of XIth International
Congress on Photosynthesis (G. Garab, edt.), Dordrecht: Kluwer Academic
Publishers, 3: 1859-1863 (1998).
Race H.L. and Hind G.
Minor constituents of photosystem II core complexes: Possible regulators of
photosystem II protein kinase.
Arch Biochem Biophys., 345:355-357 (1997).
Race H.L. and Hind G.
A protein kinase in the core of photosystem II.
Biochemistry, 35:13006-13010 (1996).
See also article in the
Brookhaven Bulletin (1996: Vol.50 No.46).
Hind G., Marshak D.R. and Coughlan S.J.
Spinach thylakoid polyphenol oxidase: cloning, characterization, and
relation to a putative protein kinase.
Biochemistry, 34:8157-8164 (1995).
France L.L., Kieleczawa J., Dunn J.J., Luft B.J., Hind G., and Sutherland J.C.
Evidence of an alpha-helical epitope on outer surface protein A from the Lyme
disease spirochete, Borrelia burgdorferi: an application of
steady-state and time-resolved fluorescence quenching techniques.
Biochim. Biophys. Acta, 1202:287-296 (1993).
Kieleczawa J., Coughlan S.J. and Hind G.
Isolation and characterization of an alkaline phosphatase from pea thylakoids.
Plant Physiol., 99:1029-1036 (1992).
Last Modified: April 17, 2009
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