Abstract:
: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.
journal_name
IUBMB Lifejournal_title
IUBMB lifeauthors
Self WT,Pierce R,Stadtman TCdoi
10.1080/15216540400010818keywords:
subject
Has Abstractpub_date
2004-08-01 00:00:00pages
501-7issue
8eissn
1521-6543issn
1521-6551pii
N2LN3QQDG49V9DRBjournal_volume
56pub_type
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