Dihydrofolate reductase protein inhibits its own translation by binding to dihydrofolate reductase mRNA sequences within the coding region Journal Article
| Authors: | Ercikan-Abali, E. A.; Banerjee, D.; Waltham, M. C.; Skacel, N.; Scotto, K. W.; Bertino, J. R. |
| Article Title: | Dihydrofolate reductase protein inhibits its own translation by binding to dihydrofolate reductase mRNA sequences within the coding region |
| Abstract: | Previous studies suggest that dihydrofolate reductase (DHFR) regulates its own translation. Moreover, intracellular levels of DHFR protein increase following exposure to the antifolate methotrexate (MTX), suggesting that MTX may release the translational inhibition mediated by DHFR [Chu et al. (1993) Biochemistry 32, 4756-4760; Ercikan et al. (1993) Adv. Exp. Med. Biol. 338, 537-540]. To further investigate the role of DHFR in translational autoregulation, we have considered the possibility that DHFR directly contacts its cognate mRNA. Binding studies using a series of truncated DHFR mRNAs as probes localized the DHFR/RNA interaction to a 100-base-pair region containing two putative stemloop structures; initial studies indicated that both of these loop structures are involved in protein binding. Moreover, the binding of MTX to DHFR prevents interaction of the protein with its cognate mRNA, thereby relieving translational autoregulation. |
| Keywords: | nonhuman; protein binding; protein stability; rna; rna-binding proteins; protein processing; transcription regulation; molecular sequence data; messenger rna; rna, messenger; rna translation; protein biosynthesis; base sequence; base pairing; binding sites; codon; dihydrofolate reductase; folic acid antagonists; tetrahydrofolate dehydrogenase; protein synthesis inhibition; rna sequence; autoregulation; cross linking; translation regulation; humans; priority journal; article; purine synthesis |
| Journal Title: | Biochemistry |
| Volume: | 36 |
| Issue: | 40 |
| ISSN: | 0006-2960 |
| Publisher: | American Chemical Society |
| Date Published: | 1997-10-07 |
| Start Page: | 12317 |
| End Page: | 12322 |
| Language: | English |
| DOI: | 10.1021/bi971026e |
| PUBMED: | 9315871 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 17 March 2017 -- Source: Scopus |
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