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)
 
 
 
 
 

Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing.

The small eukaryotic initiation factor (eIF)-4C is implicated in the initiation pathway, where it enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(i) to 40 S ribosomal subunits. In order to elucidate the function of eIF-4C, its structure has been further characterized. The amino acid sequence of many peptides from rabbit reticulocyte and wheat germ eIF-4C have been determined chemically. From the chemical sequencing of the rabbit protein, it was noted that at least two different eIF-4C molecules were present which differed by conservative substitutions at three positions (2 aspartic acid for glutamic acid switches and 1 valine for isoleucine switch). By the use of unique sequences with low codon degeneracy, primers were used to obtain a polymerase chain reaction product of appropriate size and sequence. This product was then used to isolate full-length coding sequence cDNA clones for human eIF-4C. A similar strategy was used to design PCR primers and then isolate a wheat cDNA clone which lacked the coding region for the first 23 amino acids, but contained a complete 3'-untranslated region. The protein amino acid sequence of wheat germ eIF-4C is 68% identical with the mammalian protein, and, allowing for the most conservative substitutions, the proteins are 76% similar. Both the mammalian and wheat germ proteins are 143 amino acids in length and have molecular weights of about 16,400. A unique feature of eIF-4C is its apparent "polarity" as 9 of the first 15 amino acids are basic while 13 of the last 20 amino acids are acidic. This dipole nature may enable the protein to interact with both the ribosome (perhaps via the rRNA) and other translation initiation factors.[1]

References

  1. Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing. Dever, T.E., Wei, C.L., Benkowski, L.A., Browning, K., Merrick, W.C., Hershey, J.W. J. Biol. Chem. (1994) [Pubmed]
 
WikiGenes - Universities