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

Hanley, S. Z., Pappin, D. J., Rahman, D., White, A. J., Elborough, K. M., Slabas, A. R. (March 1999) Re-evaluation of the primary structure of Ralstonia eutropha phasin and implications for polyhydroxyalkanoic acid granule binding. FEBS Letters, 447 (1). pp. 99-105. ISSN 0014-5793 (Print)0014-5793 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/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.

Item Type: Paper
Additional Information: Hanley, S Z Pappin, D J Rahman, D White, A J Elborough, K M Slabas, A R Research Support, Non-U.S. Gov't Netherlands FEBS letters FEBS Lett. 1999 Mar 19;447(1):99-105.
Uncontrolled Keywords: Alcaligenes Amino Acid Sequence Bacterial Proteins/genetics/ metabolism Base Sequence DNA, Complementary/genetics Hydroxy Acids/ metabolism Lectins/ chemistry/genetics/ 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
Subjects: bioinformatics > genomics and proteomics > design > amino acid design
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > cDNA
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
Investigative techniques and equipment > spectroscopy > mass spectrometry
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Kathleen Darby
Date: 19 March 1999
Date Deposited: 28 Apr 2014 16:05
Last Modified: 28 Apr 2014 16:05
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29814

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