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Regulation of protein synthesis in rabbit reticulocyte lysates. Thiophosphorylation of initiation factor eIF-2 by heme-regulated protein kinase.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Ranu, Rajinder Singh |
| Copyright Year | 1986 |
| Abstract | The heme-regulated protein kinase, which specifically phosphorylates the 38-kDa subunit of initiation factor eIF-2, can utilize adenosine 5'-O-(3-thiotriphosphate) (ATP[gamma S]) as a substrate. The rate of thiophosphorylation is 5-6-times slower than that observed with ATP. It is of special interest that thiophosphorylated derivatives of eIF-2 are resistant to dephosphorylation catalyzed by eIF-2 phosphoprotein phosphatase. The thiophosphorylated eIF-2 is less effective in promoting protein synthesis in hemin-deficient lysates under physiological conditions. In addition, ATP[gamma S] could also be utilized by the self-phosphorylation activity intrinsically associated with HRI. |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/0014-5793(86)81544-7 |
| PubMed reference number | 3021534 |
| Journal | Medline |
| Volume Number | 208 |
| Issue Number | 1 |
| Alternate Webpage(s) | https://core.ac.uk/download/pdf/82796880.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/0014-5793%2886%2981544-7 |
| Journal | FEBS letters |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
