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The resistance of maize plants to cold stress has been
associated with the appearance of a new chlorophyll a/b binding protein in the thylakoid membrane following chilling
treatment in the light. The cold-induced protein has been isolated,
characterized by amino acid sequencing, and pulse labeled with
radioactive precursors, showing that it is the product of
post-translational modification by phosphorylation of the minor
chlorophyll a/b protein CP29 rather than the product of a
cold-regulated gene or an unprocessed CP29 precursor. We show here that
the CP29 kinase activity displays unique characteristics differing from
previously described thylakoid kinases and is regulated by the redox
state of a quinonic site. Finally, we show that maize plants unable to
perform phosphorylation have enhanced sensitivity to cold-induced
photoinhibition.
Volume 270,
Number 15,
Issue of April 14, pp. 8474-8481, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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