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

Sequence analysis of several cDNAs encoding the phasin protein of Ralstonia eutropha indicated that the carboxyl terminus of the resulting derived pro tein sequence is different from that reported previously. This mas confirme d 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 t he binding of this protein to polyhydroxyalkanoic acid granules in the bact erium. (C) 1999 Federation of European Biochemical Societies.