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Sci. STKE, 22 October 2002
Vol. 2002, Issue 155, p. pe43
[DOI: 10.1126/stke.2002.155.pe43]


Will the Real LHC II Kinase Please Step Forward?

John F. Allen1* and Helen L. Race2

1Plant Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, Box 124, SE-221 00 Lund, Sweden.
246 Iris Close, Aylesbury, Buckinghamshire, HP21 8YZ, UK. E-mail: louise.race{at}

Abstract: Many laboratories have searched for the protein kinase responsible for phosphorylation of the chloroplast light-harvesting complex of photosynthesis, LHC II. The LHC II kinase provides a vital link in a redox signaling pathway of ecological, developmental, and evolutionary significance. Various candidates for the LHC II kinase, some stronger than others, have come and gone. Recently, a family of three thylakoid-associated kinases (TAKs) has been identified and purified; they too catalyze in vitro phosphorylation of LHC II. The LHC II kinase is part of an integrated network of signal transduction to which input is provided by a number of environmental factors. The implications of understanding these processes stretch beyond the important, central question of how plants adapt their photosynthetic machinery to changing wavelengths of light.

*Corresponding author. E-mail, john.allen{at}

Citation: J. F. Allen, H. L. Race, Will the Real LHC II Kinase Please Step Forward? Sci. STKE 2002, pe43 (2002).

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