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

S Z Hanley; D J Pappin; D Rahman; A J White; K M Elborough; A R Slabas

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

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.

Authors

S Z Hanley¹, D J Pappin, D Rahman, A J White, K M Elborough, A R Slabas

Affiliation

¹ Department of Biological Sciences, University of Durham, UK. s.z.hanley@durham.ac.uk

PMID: 10218591
DOI: 10.1016/s0014-5793(99)00235-5

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.

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

Substances

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

Associated data

GENBANK/AF079155