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

FEBS Letters

White, Andrew J¹  Pappin, Darryl J.C²  Slabas, Antoni R¹  Hanley, Steven Zachary¹  Rahman, Dinah²  Elborough, Kieran M¹ 

[1] Department of Biological Sciences, University of Durham, Durham, DH13LE, UK;Imperial Cancer Research Fund, London, WC2A 3PX, UK

关键词: Alcaligenes eutrophus;    Ralstonia eutropha;    Polyhydroxyalkanoic acid granule;    Phasin;    Biodegradable polyester;    PHA;    polyhydroxyalkanoic acid;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;    MALDI TOF MS;    matrix-assisted laser desorption/ionization time of flight mass spectrometry;    CAD;    collision-activated dissociation;   

DOI  :  10.1016/S0014-5793(99)00235-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown