FEBS Letters | |
Induction of eIF‐4E phosphorylation by the addition of L‐pyrroline‐5‐carboxylic acid to rabbit reticulocyte lysate | |
Ray, Bimal K.3  Thach, Robert E.3  Abramson, Richard D.2  Mick, Steven J.1  Hagedorn, Curt H.1  Merrick, William C.2  | |
[1] Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA;Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA;Department of Biology, Washington University, St. Louis, MO 63130, USA | |
关键词: eIF-4E; eIF-4F; mRNA cap; L-pyrroline-5-carboxylic acid; Translation; Glutathione; eIF-4F; eukaryotic initiation factor-4F (p25; p48 and p220 subunits); eIF-4E; eukaryotic initiation factor-4E (isolated p25); eIF-2; eukaryotic initiation factor-2; eIF-4A; eukaryotic initiation factor-4A; eIF-4B; eukaryotic initiation factor-4B; PAGE; polyacrylamide gel electrophoresis; IEF; isoelectric focusing; DTE; dithioerythritol; P5C; L-pyrroline-5-carboxylic acid; PP-ribose-P; 5-phosphoribosyl 1-pyrophosphate; | |
DOI : 10.1016/0014-5793(88)80082-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Addition of L-pyrroline-5-carboxylic acid to reticulocyte lysates inhibits protein synthesis and induced phosphoproteins of 25 and 14 kDa. The 25 kDa phosphoprotein had the same M r and pI as phosphorylated eIF-4E. Incubation of lysates with L-pyrroline-5-carboxylic acid did not alter the crosslinking of eIF-4E to reovirus mRNA caps. These results suggest that modifications of the translational apparatus other than eIF-4E phosphorylation may mediate the inhibitory effect seen with L-pyrroline-5-carboxylic acid and/or that phosphorylation of eIF-4E may effect functions subsequent to its interaction with the mRNA cap such as protein-protein interactions with other cap-specific translation factors.
【 授权许可】
Unknown
【 预 览 】
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