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J. Biol. Chem., Vol. 266, Issue 23, 14931-14938, Aug, 1991
J Kim, PG Klein and JE Mullet
Photosynthetic reaction center protein D1 contains five membrane- spanning
alpha-helices which form binding sites for pheophytin, chlorophyll,
carotenoids, quinone, Fe2+, and probably Mn2+. D1 translation intermediates
of 15 to 28 kD were detected when isolated chloroplasts were pulse-labeled
with [35S]methionine. The D1 translation intermediates were associated with
membrane polysomes and can be chased into full length D1. The sites of
translation pausing were determined by mapping the distribution of
ribosomes on D1 mRNA using toeprint analysis. Clusters of toeprint signals
were generated by D1 mRNA associated with membranes but not by D1 mRNA in
nonpolysomal fractions of the soluble phase or phenol-extracted mRNA. The
distribution of ribosomes on D1 mRNA determined by toeprint analysis was
consistent with D1 translation intermediates observed with pulse- labeling.
Ribosome pausing may facilitate co-translational binding of co-factors such
as chlorophyll to D1 and aid the integration of D1 into thylakoid
membranes.
Ribosomes pause at specific sites during synthesis of membrane-bound chloroplast reaction center protein D1
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128.
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