Eukaryotic protein synthesis initiation factor 2. A target for inactivation by proanthocyanidin.

Autor: Kudlicki W; Department of Chemistry and Biochemistry, University of Texas, Austin 78712., Picking WD, Kramer G, Hardesty B, Smailov SK, Mukhamedzhanov BG, Lee AV, Iskakov BK
Jazyk: angličtina
Zdroj: European journal of biochemistry [Eur J Biochem] 1991 May 08; Vol. 197 (3), pp. 623-9.
DOI: 10.1111/j.1432-1033.1991.tb15952.x
Abstrakt: Polyproanthocyanidin (PPA), a phenolic polymer isolated from the plant Alhagi kirgisorum S. was found to interact strongly with eukaryotic initiation factor 2 (eIF-2), thereby inhibiting reactions involving this protein. When added to a rabbit reticulocyte lysate system, PPA blocks in vitro translation and it appears to selectively bind and precipitate a relatively small number of proteins including eIF-2 and regulin. The phosphorylation of purified regulin and eIF-2 by casein kinase II (CK II) and the heme-sensitive eIF-2 alpha kinase, respectively, was also inhibited by the polyphenolic compound. The natural fluorescence of PPA was utilized to compare its interaction with eIF-2 and regulin to that with other natural and synthetic polypeptides.
Databáze: MEDLINE