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PMID: 2211706 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

The Journal of biological chemistry ·Vol. 265 ·No. 30 ·1990-10-25 ·Pages 18339-44

Ragland M, Briat JF, Gagnon J, Laulhere JP, Massenet O, Theil EC

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.

MeSH Terms
Amino Acid Sequence Base Sequence Chloroplasts/physiology Cloning, Molecular DNA/genetics Fabaceae/genetics Ferritins/genetics Molecular Sequence Data Peptide Fragments/chemistry Plant Proteins/genetics Plants, Medicinal RNA, Messenger/genetics Soybeans/genetics
Chemicals
Peptide Fragments Plant Proteins RNA, Messenger DNA Ferritins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Ragland M
Department of Biochemistry, North Carolina State University, Raleigh 27695-7622.
Briat J F
Gagnon J
Laulhere J P
Massenet O
Theil E C
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1990-10-25
Pages
18339-44
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIDDK NIH HHS · DK 20251 · United States
Databases
GENBANK
J05656, M58336
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