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)
 

Links

 

Gene Review

EF2  -  Elongation factor 2

Drosophila melanogaster

Synonyms: CG2238, Dmel\CG2238, EF-2, EF-2b, EF2b, ...
 
 
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.
 

High impact information on Ef2b

  • This identification was based on the high degree of its amino acid sequence identity (greater than 80%) to that of hamster EF2 [1].
  • Conserved sequence segments shared with a variety of GTP binding proteins are found in the amino terminal third of the protein, and segments unique to EF2 and its prokaryotic functional homolog, EF-G, are in the carboxy terminal half; these two regions are segregated in two respective exons [1].
  • The gene encoding Drosophila EF2 is found at position 39E-F of the 2L chromosomal arm and maybe identical to the M(2)H locus, which produces a Minute phenotype when mutated [1].
  • Because DTM fortuitously bears the same point mutation as found in the A chain of CRM197, an ADP-ribosyltransferase (ADPrT)-deficient form of DTx, we hypothesized that the dramatic low-temperature-sensitive effects did not stem from ADP-ribosylation of elongation factor 2 (EF-2) [2].
  • Phylogenies were inferred from both the gene and the protein sequences of the translational elongation factor termed EF-2 (for Archaea and Eukarya) and EF-G (for Bacteria) [3].
 

Associations of Ef2b with chemical compounds

  • However, the histidyl residue target for ADP-ribosylation of EF-2 by diphtheria toxin is replaced by tyrosine in EFT-1 [4].
 

Analytical, diagnostic and therapeutic context of Ef2b

  • Sequence analysis of genomic and cDNA clones revealed that the deduced amino acid sequence of the protein (EFT-1) is 38% identical to that of mammalian and Drosophila elongation factor 2 (EF-2) [4].
  • Amplification of fragments encoding highly conserved regions of EF-2 using the polymerase chain reaction led to the isolation of a fragment encoding the modifiable histidyl residue and which likely represents part of the C. elegans EF-2 gene (eft-2) [4].

References

  1. Isolation and characterization of the Drosophila translational elongation factor 2 gene. Grinblat, Y., Brown, N.H., Kafatos, F.C. Nucleic Acids Res. (1989) [Pubmed]
  2. Characterization of a cloned temperature-sensitive construct of the diphtheria toxin A domain. Lee, J.W., Cho, E., Aghaian, E., Aghaian, E., Der, J., Wisnieski, B.J. Biochemistry (2005) [Pubmed]
  3. Early evolutionary relationships among known life forms inferred from elongation factor EF-2/EF-G sequences: phylogenetic coherence and structure of the archaeal domain. Cammarano, P., Palm, P., Creti, R., Ceccarelli, E., Sanangelantoni, A.M., Tiboni, O. J. Mol. Evol. (1992) [Pubmed]
  4. Isolation and characterization of eft-1, an elongation factor 2-like gene on chromosome III of Caenorhabditis elegans. Ofulue, E.N., Candido, E.P. DNA Cell Biol. (1992) [Pubmed]
 
WikiGenes - Universities