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Originally published In Press as doi:10.1074/jbc.M009236200 on November 13, 2000
J. Biol. Chem., Vol. 276, Issue 5, 3476-3483, February 2, 2001
Light-associated and Processing-dependent Protein
Binding to 5' Regions of rbcL mRNA in the
Chloroplasts of a C4 Plant*
Dennis J.
McCormac ,
Hanz
Litz,
Jianxin
Wang,
Paul D.
Gollnick, and
James O.
Berry§
From the Department of Biological Sciences, State University of New
York, Buffalo, New York 14260
In amaranth, a C4
dicotyledonous plant, the plastid rbcL gene (encoding the
large subunit of ribulose-1,5-bisphosphate carboxylase) is regulated
post-transcriptionally during many developmental processes, including
light-mediated development. To identify post-transcriptional regulators
of rbcL expression, three types of analyses (polysome heel
printing, gel retardation, and UV cross-linking) were utilized. These
approaches revealed that multiple proteins interact with 5' regions of
rbcL mRNA in light-grown, but not etiolated, amaranth plants. Light-associated binding of a 47-kDa protein (p47), observed by
UV cross-linking, was highly specific for the rbcL 5' RNA. Binding of p47 occurred only with RNAs corresponding to mature processed rbcL transcripts (5'-untranslated region (UTR)
terminating at 66); transcripts with longer 5'-UTRs did not associate
with p47 in vitro. Variations in the length of the
rbcL 5'-UTR were found to occur in vivo, and
these different 5' termini may prevent or enhance light-associated p47
binding, possibly affecting rbcL expression as well. p47
binding correlates with light-dependent rbcL
polysome association of the fully processed transcripts in photosynthetic leaves and cotyledons but not with cell-specific rbcL mRNA accumulation in bundle sheath and mesophyll chloroplasts.
*
This work was supported by National Science Foundation
Grants MCB 9316806 (to J. O. B.) and MCB 9728547 (to J. O. B. and
P. D. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Imaging Research, Inc., Brock University, St.
Catherines, ON, CA.
§
To whom correspondence should be addressed. Tel.: 716-645-3488;
Fax: 716-645-2975; E-mail: camjob@acsu.buffalo.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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