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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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Characterization of active dipeptide transport by germinating barley embryos: Effects of pH and metabolic inhibitors.

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Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides.

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Peptide transport by germinating barley embryos: Evidence for a single common carrier for di- and oligopeptides.

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Stereospecificity of peptide transport by germinating barley embryos.

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Peptide transport by germinating barley embryos.

C F Higgins1, J W Payne

  • 1Department of Botany, Science Laboratories, University of Durham, South Road, DH1 3LE, Durham, U.K..

Planta
|January 15, 2014
PubMed
Summary

Germinating barley embryos actively transport intact glycylsarcosine, a peptidase-resistant dipeptide. This provides the first evidence of a dipeptide transport system facilitating nutrient movement from endosperm to embryo during germination.

Area of Science:

  • Plant Physiology
  • Molecular Biology
  • Biochemistry

Background:

  • Plant germination relies on nutrient mobilization from storage tissues.
  • Peptidases break down proteins into amino acids for embryo uptake.
  • The transport of intact dipeptides in plants remains largely uncharacterized.

Purpose of the Study:

  • To investigate the transport of dipeptides in germinating barley embryos.
  • To determine if glycylsarcosine is transported intact across the scutellum.
  • To identify potential dipeptide transport systems in plants.

Main Methods:

  • Using germinating embryos of Hordeum vulgare L., var. Maris Otter, Winter.
  • Monitoring the accumulation of glycylsarcosine against a concentration gradient.

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  • Analyzing the integrity of glycylsarcosine post-transport.

    • Main Results:

    • Glycylsarcosine, a dipeptide resistant to peptidase activity, was accumulated intact.
    • Accumulation occurred against a concentration gradient, indicating active transport.
    • This demonstrates the presence of a functional dipeptide transport system.

    Conclusions:

    • Hordeum vulgare embryos possess a dipeptide transport system.
    • This system is crucial for transferring intact dipeptides from the endosperm to the embryo.
    • This finding offers new insights into nutrient mobilization during plant germination.