Re-evaluation of the primary structure of Ralstonia eutropha phasin and implications for polyhydroxyalkanoic acid granule binding

FEBS Lett. 1999 Mar 19;447(1):99-105. doi: 10.1016/s0014-5793(99)00235-5.


Sequence analysis of several cDNAs encoding the phasin protein of Ralstonia eutropha indicated that the carboxyl terminus of the resulting derived protein sequence is different from that reported previously. This was confirmed by: (1) sequencing of the genomic DNA; (2) SDS-PAGE and peptide analysis of wild-type and recombinant phasin; and (3) mass spectrometry of wild-type phasin protein. The results have implications for the model proposed for the binding of this protein to polyhydroxyalkanoic acid granules in the bacterium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcaligenes
  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • DNA, Complementary / genetics
  • Hydroxy Acids / metabolism*
  • Lectins / chemistry*
  • Lectins / genetics
  • Lectins / metabolism*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Plant Lectins*
  • Polymerase Chain Reaction
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Sequence Analysis
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization


  • Bacterial Proteins
  • DNA, Complementary
  • Hydroxy Acids
  • Lectins
  • Peptide Fragments
  • Plant Lectins
  • Recombinant Proteins
  • phasin

Associated data

  • GENBANK/AF079155