Ptushkina, Marina and Berthelot, K. and von der Haar, Tobias and Geffers, L. and Warwicker, J. and McCarthy, John E. G. (2001) A Second eIF4E Protein in Schizosaccharomyces Pombe has Distinct eIF4G-binding Properties. Nucleic Acids Research, 29 (22). pp. 4561-4569. ISSN 0305-1048. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
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The eukaryotic cap-binding proteins belonging to the eIF4E family are generally involved in mediating the recruitment of ribosomes to capped mRNA. We described previously a cap-binding protein (now called eIF4E1) in Schizosaccharomyces pombe that appears to have all of the usual structural and functional attributes of an eIF4E. We have now characterised a new type of cap-binding protein (eIF4E2) from this organism, which at the amino acid sequence level, is 52% identical and 59% similar to eIF4E1. eIF4E2 is not essential in S.pombe but has some novel properties that may be related to a special function in the cell. The ratio of eIF4E2:eIF4E1 in the cell shifts in favour of eIF4E2 at higher temperatures. Despite having all of the dorsal face amino acids that have so far been associated with eIF4G binding to eIF4E1, eIF4E2 binds the eIF4E-binding domain of S.pombe eIF4G >10(2)-times weaker than eIF4E1 in vitro. The eIF4E2 cap-binding affinity is in the typical micromolar range. The results suggest that eIF4E2 is not active on the main pathway of translation initiation in fission yeast but might play a role in the adaptation strategy of this organism under specific growth conditions. Moreover, they provide insight into the molecular characteristics required for tight binding to eIF4G.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Tobias von der Haar|
|Date Deposited:||30 Sep 2008 18:37|
|Last Modified:||11 Jun 2014 10:43|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/5340 (The current URI for this page, for reference purposes)|