Cloning and heterologous expression of a Methanococcus vannielii gene encoding a selenium-binding protein.

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 Life

journal_title

IUBMB life

authors

Self WT,Pierce R,Stadtman TC

doi

10.1080/15216540400010818

keywords:

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

501-7

issue

8

eissn

1521-6543

issn

1521-6551

pii

N2LN3QQDG49V9DRB

journal_volume

56

pub_type

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