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(Received for publication, July 25, 1995; and in revised form, October 19, 1995)
We have examined the effects of illumination, carbon source, and
levels of chloroplast protein synthesis on trans-acting proteins that
bind to the leaders of five representative chloroplast mRNAs. The
accumulation of these five chloroplast mRNAs and the proteins they
encode were measured in cells grown under identical conditions.
Extracts from all cell types examined contain a minimum set of six
chloroplast 5`-untranslated region (UTR)-binding proteins (81, 62, 56,
47, 38, and 15 kDa). Fractionation results suggest that multiple forms
of the 81-, 62-, and 47-kDa proteins may exist. A 36-kDa protein was
found in all cells except those deficient in chloroplast protein
synthesis. Binding of the 81-, 47-, and 38-kDa proteins to the rps12 leader is effectively competed by the atpB or rbcL 5`-UTRs, indicating that the same proteins bind to all
three leaders. In contrast, these three proteins do not bind to the
nuclear-encoded 
-1 tubulin leader, which bound novel
proteins of 110, 70, and 43 kDa. Cis-acting sequences within the
5`-UTRs of two chloroplast mRNAs (rps7 and atpB) have
been identified which are protected from digestion by RNase T1 by
extracts enriched for the 81-, 47-, and 38-kDa proteins.
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