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.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Examination of the signal peptide region of human biotinidase using a baculovirus expression system.

Biotinidase deficiency is an autosomal recessive disorder of biotin recycling. Biotinidase cleaves the biotin from biocytin or short biotinyl-peptides to replenish the free biotin pool, or it can transfer the vitamin to specific proteins. The cDNA for human serum biotinidase has two in-frame start codons, potentially allowing for the synthesis of an enzyme with a signal peptide (SP) consisting of either 21 or 41 amino acids. In order to examine the requirements of the signal peptide region for the production and secretion of biotinidase, three different forms of the normal human serum biotinidase gene were constructed that encode either the 21-amino-acid SP (SP21-NL) or the 41-amino-acid SP (SP41-NL) or without a SP (NoSP-NL). These constructs were expressed in insect cells via a baculovirus expression system. Biotinidase from cells with SP41-NL and SP21-NL had immunoreactive and biotinyl-hydrolase-active enzyme in lysates and expression media. Cells with NoSP-NL had about 3% of the immunoreactive material and no enzyme activity in lysates and no immunoreactive protein or enzymatic activity in the expression medium. Lack of biotinidase from cells with NoSP-NL may be due to translation inefficiency or increased susceptibility of this species to protease degradation than the secreted forms. We have demonstrated that the 21-amino-acid signal peptide is sufficient to result in glycosylated, secreted biotinidase, but we cannot determine if the glycosylated biotinidase in the lysates or secreted in the medium of cells with SP41-NL use the first, second, or both ATGs in the SP region. Because this particular expression system has no mechanism for timing the movement of newly translated biotinidase protein, we cannot draw conclusions about the relative efficiency of SP41-NL versus SP21-NL, but it is possible that either is used in vivo depending on particular cellular conditions.[1]


WikiGenes - Universities