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

Abstract

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.

Keywords

RalstoniaChemistryGranule (geology)Protein primary structureBiochemistryPrimary (astronomy)BiologyPeptide sequenceEnzymePhysics

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Publication Info

Year: 1999
Type: article
Volume: 447
Issue: 1
Pages: 99-105
Citations: 46
Access: Closed

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APA Style

                            
                                
                                    Zac Hanley, 
                                
                                    Darryl Pappin, 
                                
                                    Dinah Rahman
                                
                                et al.
                            
                            (1999). 
                            Re‐evaluation of the primary structure of <i>Ralstonia eutropha</i> phasin and implications for polyhydroxyalkanoic acid granule binding. 
                            FEBS Letters
                            , 447
                            (1)
                            , 99-105.
                            https://doi.org/10.1016/s0014-5793(99)00235-5
                        

Identifiers

DOI: 10.1016/s0014-5793(99)00235-5