Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening

Nat Biotechnol. 1998 May;16(5):473-7. doi: 10.1038/nbt0598-473.

Abstract

We have cloned a gene involved in starch metabolism that was identified by the ability of its product to bind to potato starch granules. Reduction in the protein level of transgenic potatoes leads to a reduction in the phosphate content of the starch. The complementary result is obtained when the protein is expressed in Escherichia coli, as this leads to an increased phosphate content of the glycogen. It is possible that this protein is responsible for the incorporation of phosphate into starch-like glucans, a process that is not understood at the biochemical level. The reduced phosphate content in potato starch has some secondary effects on its degradability, as the respective plants show a starch excess phenotype in leaves and a reduction in cold-sweetening in tubers.

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular
  • Cold Temperature*
  • DNA, Plant / chemistry
  • DNA, Plant / genetics
  • Escherichia coli / genetics
  • Genetic Engineering
  • Glycogen / chemistry
  • Molecular Sequence Data
  • Phenotype
  • Phosphates / analysis
  • Plant Leaves / chemistry
  • Plant Leaves / genetics
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plants, Genetically Modified
  • Solanum tuberosum / genetics
  • Starch / analysis
  • Starch / genetics
  • Starch / metabolism*

Substances

  • DNA, Plant
  • Phosphates
  • Plant Proteins
  • Starch
  • Glycogen

Associated data

  • GENBANK/Y09533