Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

selB - selenocysteinyl-tRNA-specific translation...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3579, JW3563, fdhA

Forchhammer, K. et al., Kromayer, M. et al., Gr??be, T. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of selB

The product of the selB gene from Escherichia coli is required for co-translational insertion of selenocysteine into protein [1].
To make the SELB protein accessible to biochemical analysis, the protein was purified from cells that overexpressed the selB gene from a phage T7 promoter plasmid [1].
To gain information on the domain structure of this specialized translation factor, the selB genes from two bacteria unrelated to Escherichia coli (Clostridium thermoaceticum and Desulfomicrobium baculatum) were cloned and sequenced [2].

High impact information on selB

The N-terminal amino acid sequence of the purified protein was determined, and it confirmed that the initiation codon of selB mRNA translation overlaps the stop codon of the preceding selA gene by 4 bases [1].
GrdB could be heterologously produced in Escherichia coli with coexpression of selB and selC from E. acidaminophilum for selenocysteine insertion [3].

References

Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis. Forchhammer, K., Rücknagel, K.P., Böck, A. J. Biol. Chem. (1990) [Pubmed]
Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB. Kromayer, M., Wilting, R., Tormay, P., Böck, A. J. Mol. Biol. (1996) [Pubmed]
Peroxidase activity of selenoprotein GrdB of glycine reductase and stabilisation of its integrity by components of proprotein GrdE from Eubacterium acidaminophilum. Gr??be, T., Reuter, M., Gursinsky, T., S??hling, B., Andreesen, J.R. Arch. Microbiol. (2007) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.