Eukaryotic protein synthesis initiation factor 2. A target for inactivation by proanthocyanidin.
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.
Kudlicki
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W
Department of Chemistry and Biochemistry, University of Texas, Austin 78712.
Picking
W D
WD
Kramer
G
G
Hardesty
B
B
Smailov
S K
SK
Mukhamedzhanov
B G
BG
Lee
A V
AV
Iskakov
B K
BK
D000818:Animals; D000872:Anthocyanins / Q000494:pharmacology*; D047388:Casein Kinases; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism*; D010766:Phosphorylation; D044945:Proanthocyanidins; D014176:Protein Biosynthesis; D011494:Protein Kinases / Q000494:pharmacology; D011817:Rabbits
D000872:Anthocyanins; D003598:Cytoskeletal Proteins; D015852:Eukaryotic Initiation Factor-2; D044945:Proanthocyanidins; C013221:proanthocyanidin; D011494:Protein Kinases; D047388:Casein Kinases