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Plant Physiol, February 2001, Vol. 125, pp. 770-778
The 5' End of the Pea Ferredoxin-1 mRNA Mediates Rapid and
Reversible Light-Directed Changes in Translation in
Tobacco1
Eric R.
Hansen,
Marie E.
Petracek,2*
Lynn F.
Dickey,3 and
William F.
Thompson
Department of Botany, North Carolina State University, Raleigh,
North Carolina 27695
Ferredoxin-1 (Fed-1) mRNA contains an
internal light response element (iLRE) that destabilizes mRNA when
light-grown plants are placed in darkness. mRNAs containing this
element dissociate from polyribosomes in the leaves of transgenic
tobacco (Nicotiana tabacum) plants transferred to the
dark for 2 d. Here, we report in vivo labeling experiments with a
chloramphenicol acetyl transferase mRNA fused to the
Fed-1 iLRE. Our data indicate that the
Fed-1 iLRE mediates a rapid decline in translational
efficiency and that iLRE-containing mRNAs dissociate from polyribosomes
within 20 min after plants are transferred to darkness. Both events
occur before the decline in mRNA abundance, and polyribosome
association is rapidly reversible if plants are re-illuminated. These
observations support a model in which Fed-1 mRNA in
illuminated leaves is stabilized by its association with polyribosomes,
and/or by translation. In darkness a large portion of the mRNA
dissociates from polyribosomes and is subsequently degraded. We also
show that a significant portion of total tobacco leaf mRNA is shifted
from polyribosomal to non-polyribosomal fractions after 20 min in the
dark, indicating that translation of other mRNAs is also rapidly
down-regulated in response to darkness. This class includes some, but
not all, cytoplasmic mRNAs encoding proteins involved in photosynthesis.
1
This work was supported by the National Science
Foundation (grant no. MCB-9507396), the National Institutes of Health
(grant no. GM43108 to W.F.T. and L.F.D.), and the U.S. Department of Agriculture (grant no. 98-35301-7012 to M.E.P.). E.R.H. was supported by the U.S. Department of Education, Graduate Assistance in Areas of
National Need-Interdisciplinary Doctoral Program in Biotechnology. This
research was supported by the Oklahoma Agricultural Experiment Station
(project no. H-2427).
2
Present address: 246 NRC, Oklahoma State University,
Stillwater, OK 74078.
3
Present address: Biolex, 480 Hillsboro Street, Suite
100, Pittsboro, NC 27312.
*
Corresponding author; e-mail
marie petracek{at}biochem.okstate.edu; fax 405-744-7799.
© 2001 American Society of Plant Physiologists
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