Characterization of a single copy gene encoding ferredoxin I from pea.

Elliott, Robert C.; Pedersen, Thomas J.; Fristensky, Brian; White, Michael J.; Dickey, Lynn F.; Thompson, William F.

doi:10.1105/tpc.1.7.681

Cited by 56 publications

(43 citation statements)

References 33 publications

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“…, 1990;Vorst eta/., 1990). Binding of nuclear proteins to a -23 to -494 promoter fragment of the pea Fed4 gene was shown in gel retardation experiments (Elliott et a/., 1989a). The pea RbcS-3A promoter was not an effective competitor for binding, indicating the presence of proteins binding to the Fed4 but not to the RbcS-3A promoter.…”

Section: Introductionmentioning

confidence: 99%

Light-regulated expression of the Arabidopsis thaliana ferredoxin A gene involves both transcriptional and post-transcriptional processes

Vorst¹,

Dam²,

Weisbeek³

et al. 1993

Plant J

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SummaryFerredoxin is part of the photosynthetic apparatus of the chloroplast and is encoded in the nucleus. In Arabidopsis thaliana expression of the ferredoxin A gene is influenced by both the presence of chloroplasts and light. Tobacco plants transformed with a ferredoxin promoter-GUS fusion gene showed a tissue-specific and light-dependent expression pattern. The effect of light on the expression of the fusion gene in transgenic seedlings was only two-to fourfold, which is less pronounced than the 20-fold effect in Arabidopsis itself. Run-on transcription assays with nuclei isolated from Arabidopsis revealed a twofold modulation of transcriptional activity of the ferredoxin A gene under the influence of light. These results suggest the involvement of post-transcriptional processes in lightregulated gene expression.A ferredoxin promoter deletion series ranging from -1205 to -143 was studied. All but the smallest deletion construct (at position -143 relative to the translation start site) showed comparable expression levels in mature leaves, suggesting the presence of a positive regulating element between -269 and -143. The same pattern of tissue specificity was found in all promoter deletions studied. Expression of the fusion genes is high in all chloroplast-containing cells: mesophyll, chlorenchyma, paravascular tissue, epidermal and stomata1 guard cells and trichomes. Transgenic seedlings treated with norflurazon, which blocks the development of green chloroplasts, showed a two-to fourfold reduction in GUS expression for all constructs. In Arabidopsis seedlings the effect of norflurazon on the expression of the ferredoxin A was eightfold. This again can be explained by the need for post-transcriptional processes of the regulated gene expression of Arabidopsis ferredoxin A.

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Section: Introductionmentioning

confidence: 99%

Light-regulated expression of the Arabidopsis thaliana ferredoxin A gene involves both transcriptional and post-transcriptional processes

Vorst¹,

Dam²,

Weisbeek³

et al. 1993

Plant J

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“…Since the structure of the amino-terminal transit peptide of Fd III is very different from those of leaf-specific, chloroplast-localized Fds from maize (9) and other plants (7,22,23,29), and since no data have been obtained on the subcellular localization of Fd in nonphotosynthetic cells, it is difficult to predict whether the transit peptide may function as a signal for targeting to plastids or other organelles. This study presents the first biochemical evidence that Fd distributed in various parts of the plant, including nonphotosynthetic organs, is able to become localized in plastids.…”

Section: Discussionmentioning

confidence: 97%

Plastid Import and Iron-Sulfur Cluster Assembly of Photosynthetic and Nonphotosynthetic Ferredoxin Isoproteins in Maize

Suzuki¹,

Izumihara²,

Hase³

1991

Plant Physiol.

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We have previously isolated and characterized two cDNAs of maize (Zea mays) ferredoxin (Fd) isoproteins, which are differentially expressed in photosynthetic and nonphotosynthetic organs, and in response to illumination of the developing seedlings (Hase T, Kimata Y, Yonekura K, Matsumura T, Sakakibara H [1991] Plant Physiol 96: 77-83). To clarify the biosynthetic pathway of Fds present in the different organs, precursors of the two Fd isoproteins synthesized by in vitro transcription and translation were examined to determine whether they are imported to chloroplasts and etioplasts. Precursors for both Fd I and Fd Ill, a leafspecific, photosynthetic isoprotein and a constitutive, nonphotosynthetic one, respectively, were imported into chloroplasts and processed to the mature size. Some of the mature-sized molecules inside the organelles were found to be assembled with an iron-sulfur cluster. The cluster assembly occurred without tight coupling to the translocation and processing steps of the protein import, and the process was time and temperature dependent and did not require light. Etioplasts were also capable of importing the precursor of Fd IlIl and assembling the cluster. These combined data show that the constitutive, nonphotosynthetic Fd has the ability to become localized in plastids as a functional molecule.Fds are acidic, low mol wt, soluble iron-sulfur proteins found in various organisms, and act as multifunctional electron carriers in diverse redox systems. In higher plants, Fds are mainly distributed in photosynthetic organs and occupy key positions for partitioning photo-reducing power to many metabolic processes (2). They are also present in nonphotosynthetic organs such as roots (12,25,27), and it is generally assumed that nonphotosynthetic Fds are probably involved in electron transfer from pyridine dinucleotides to some Fdlinked enzymes (25,27).

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“…In pea, the nuclear-encoded photosynthetic electron transport protein ferredoxin 1 is encoded by the singlecopy, intronless Fed-1 gene (Elliott et al, 1989) and is transported into the chloroplast to facilitate electron transfer from photosystem 1 to NADP ϩ . Expression from Fed-1 is controlled by an internal light-regulatory element (iLRE) present within the transcript that regulates the stability of the mRNA .…”

Section: Introductionmentioning

confidence: 99%

Heat Shock Protein HSP101 Binds to the Fed-1 Internal Light Regulatory Element and Mediates Its High Translational Activity

et al. 2000

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The internal light-regulatory element (iLRE) of ferredoxin ( Fed-1 ) mRNA, comprising the 5 Ј leader and at least the first 13 codons of the open reading frame, controls transcript abundance after illumination of the plant in a translationdependent manner. We have characterized the RNA binding activities associated with the Fed-1 iLRE and have identified one activity as the heat shock protein HSP101, a protein shown to bind the 5 Ј leader of tobacco mosaic virus. HSP101 was sufficient and necessary to mediate a high level of translational activity from a Fed-1 iLRE-containing mRNA in yeast. Moreover, the Fed-1 iLRE substantially enhanced translation of reporter mRNAs in plant protoplasts expressing HSP101. Expression of HSP101 was subject to developmental regulation in leaves in that expression was highest in young leaves. These data suggest that Fed-1 mRNA may use the HSP101 regulatory mechanism as a means of ensuring a high level of translation required for the light-mediated regulation of Fed-1 mRNA stability.

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Characterization of a single copy gene encoding ferredoxin I from pea.

Cited by 56 publications

References 33 publications

Light-regulated expression of the Arabidopsis thaliana ferredoxin A gene involves both transcriptional and post-transcriptional processes

Light-regulated expression of the Arabidopsis thaliana ferredoxin A gene involves both transcriptional and post-transcriptional processes

Plastid Import and Iron-Sulfur Cluster Assembly of Photosynthetic and Nonphotosynthetic Ferredoxin Isoproteins in Maize

Heat Shock Protein HSP101 Binds to the Fed-1 Internal Light Regulatory Element and Mediates Its High Translational Activity

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