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Cloning and Heterologous Expression of a Methanococcus vannielii Gene Encoding a Selenium‐Binding Protein
Author(s) -
Self William,
Pierce Renee,
Stadtman TC
Publication year - 2004
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540400010818
Subject(s) - selenocysteine , formate dehydrogenase , methanococcus , biochemistry , operon , selenium , heterologous expression , gene , hspa2 , biology , escherichia coli , chemistry , microbiology and biotechnology , formate , peptide sequence , recombinant dna , enzyme , cysteine , organic chemistry , catalysis
The activation and incorporation of selenium into selenocysteine containing selenoproteins has been well established in an Escherichia coli model system but there is little specific information concerning the transport and intracellular trafficking of selenium in biological systems in general. A selenium transport role is a possible function of a novel 42 kDa selenium‐binding protein that recently was purified from Methanococcus vannielii. The gene encoding a monomer of this protein (Sbp) has been cloned, sequenced and heterologously expressed in E. coli. The 8.8 kDa gene product contains 81 amino acids. The recombinant Sbp (rSbp) protein was shown to bind selenium from added selenite. The bound selenium appeared predominantly in dimeric and tetrameric forms of the protein. The gene encoding Sbp occurs in an operon that contains a carbonic anhydrase gene and selenocysteine‐containing formate dehydrogenase genes, suggesting possible roles in selenium‐dependent formate metabolism. IUBMB Life, 56: 501‐507, 2004