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 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.
Hanley
S Z
SZ
Department of Biological Sciences, University of Durham, UK. s.z.hanley@durham.ac.uk
Pappin
D J
DJ
Rahman
D
D
White
A J
AJ
Elborough
K M
KM
Slabas
A R
AR
D000421:Alcaligenes; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D006880:Hydroxy Acids / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D037121:Plant Lectins; D016133:Polymerase Chain Reaction; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D017421:Sequence Analysis; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D001426:Bacterial Proteins; D018076:DNA, Complementary; D006880:Hydroxy Acids; D037102:Lectins; D010446:Peptide Fragments; D037121:Plant Lectins; D011994:Recombinant Proteins; C008825:phasin