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Manduca sexta hemolymph ferritin: cDNA sequence and mRNA expression

D Q Pham1, D Zhang, D H Hufnagel

  • 1Department of Biochemistry, University of Arizona, Tucson 85721, USA. Pham@biosci.arizona.edu

Gene
|June 26, 1996
PubMed
Summary

Researchers identified and sequenced a Manduca sexta (Ms) hemolymph ferritin (Fer) subunit. This insect ferritin shares similarities with vertebrate light-chain subunits and has a potential iron-responsive element, suggesting conserved iron regulation mechanisms.

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Area of Science:

  • * Molecular Biology
  • * Biochemistry
  • * Entomology

Background:

  • * Ferritin (Fer) is a protein complex responsible for iron storage in cells.
  • * Understanding insect ferritin is crucial for comparative studies of iron metabolism.
  • * The tobacco hornworm, Manduca sexta, serves as a model organism in insect physiology research.

Purpose of the Study:

  • * To identify and characterize the cDNA encoding the hemolymph ferritin subunit from Manduca sexta.
  • * To investigate potential iron-regulatory elements in the Manduca sexta ferritin mRNA.
  • * To compare the structural and functional characteristics of Manduca sexta ferritin with vertebrate ferritins.

Main Methods:

  • * cDNA cloning and nucleotide sequencing of the Manduca sexta ferritin subunit.

Related Experiment Videos

  • * Deduced amino acid sequence analysis and comparison with vertebrate ferritin sequences.
  • * Northern blot analysis to determine ferritin mRNA expression patterns in different tissues.

    • Main Results:

    • * A cDNA clone for the Manduca sexta hemolymph ferritin (Ms Fer) subunit was successfully sequenced.
    • * The deduced Ms Fer subunit sequence exhibits approximately 50% similarity to vertebrate ferritin subunits.
    • * A potential iron-responsive element (IRE) stem-loop structure was identified in the 5' untranslated region of the Ms Fer mRNA.
    • * Ms Fer subunit lacks key residues for rapid iron biomineralization and conserved ferroxidase centers, suggesting resemblance to vertebrate light-chain ferritin.
    • * Ferritin mRNA expression is highest in the midgut, with lower levels in fat body and hemocytes.

    Conclusions:

    • * The Manduca sexta hemolymph ferritin subunit shares conserved features with vertebrate ferritins, particularly the light-chain subunit.
    • * The presence of a putative IRE suggests conserved mechanisms for regulating ferritin synthesis in response to iron levels.
    • * Differential expression of ferritin mRNA in various tissues indicates tissue-specific roles in iron homeostasis within the insect.