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Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean.

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Ragland, M, Briat, J F, Gagnon, J, Laulhere, J P, Massenet, O, Theil, E C·1990·Journal of Biological Chemistry

Abstract

Ferritin is a large multisubunit protein that stores iron in plants, animals, and bacteria. In animals, the protein is mainly cytoplasmic and is highly conserved, while in plants ferritin is found in chloroplasts and other plastids. Ferritin is synthesized in plants as a larger precursor of the mature subunit. There is no sequence information for ferritin from plants, except an NH2-terminal peptide of 35 residues which shows little similarity to any known ferritin sequences or transit peptides (Laulhere, J. P., Laboure, A. M., and Briat, J. F. (1989) J. Biol. Chem. 264, 3629-3635). To understand the genetic origin and the location of ferritin synthesis in plant cells, as well as the structure of ferritin from plants, we have sequenced both CNBr peptides from pea seed ferritin and nucleotides of a soybean hypocotyl ferritin cDNA, identified using a frog ferritin cDNA as a probe. Comparison of pea and soybean sequences showed an identity of 89%. Alignment of the plant ferritin sequences with animal ferritins showed 55-65% sequence identity in the common regions. However, a peptide of 28 amino acids extended the NH2 terminus of the plant ferritins. Furthermore, the cDNA encoded additional amino acids which appear to be a transit peptide. None of the sequences in soybean ferritin were found in the tobacco chloroplast genome, suggesting, as does the transit peptide, a nuclear location of ferritin gene(s) in plants. Plant ferritin mRNA is 400-500 nucleotides longer than animal ferritin mRNAs, a difference accounted for in part by the extra peptides encoded. The size of soybean ferritin mRNA was constant in different tissues but expression varied in different tissues (leaf greater than hypocotyl). Thus, higher plants and animal ferritins display sequence homology and differential tissue expression. An ancient, common progenitor apparently gave rise to contemporary eukaryotic ferritins after specific modifications, e.g. transport to plasmids.

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Metadata

Authors
Ragland, M., Briat, J. F., Gagnon, J., Laulhere, J. P., Massenet, O., & Theil, E. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1990-10
Volume
265
Issue
30
Pages
18339-18344
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1519124463
Cited by
166
References
0
FWCI
13.83
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. https://app.cochat.ai/papers/10.1016/s0021-9258(17)44757-0
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Ragland, M., Briat, J. F., Gagnon, J., Laulhere, J. P., Massenet, O., & Theil, E. C. (1990). Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)44757-0

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