Characteristics of the translation of thymosin alpha 1 precursor mRNA by cell-free wheat germ system. Evidence for the acetylation of thymosin alpha 1 precursor.
Nogueira. M M; Freire. M M
Key Findings
- Thymosin‑alpha‑1 precursor mRNA translates efficiently in a wheat‑germ cell‑free system
- Spermidine increases the translation rate of the mRNA, modulated by magnesium
- The newly made thymosin‑alpha‑1 precursor is acetylated during biosynthesis
Practical Outcomes
- For biohackers this study offers little direct guidance on using thymosin‑alpha‑1. It mainly confirms that the natural peptide is acetylated, a detail that might influence its activity, but it does not suggest new dosing, formulation, or performance‑enhancing protocols.
Summary
The paper shows that the mRNA for thymosin‑alpha‑1 can be efficiently made into protein in a wheat‑germ cell‑free system, that the polyamine spermidine speeds up the translation, and that the peptide gets an acetyl group attached during its synthesis.
Abstract
At the optimal concentrations of Mg2+ and K+ to translate total thymus PolyA+-RNA, the purified thymosin alpha 1 precursor mRNA saturate the protein synthetic activity at lower concentration than the total thymus mRNAs. The polyamine spermidine increases the translation rate of the messenger, which is modulated by magnesium, rather than improve the yield in full-length chains of thymosin alpha 1 precursor. As other eukariotic mRNAs, this messenger presents the "cap" modification at the 5'-end terminal position. The incorporation of [3H]acetate into the translation product of the messenger, shows an evidence for the acetylation of the thymosin alpha 1 precursor during its biosynthesis in vitro.
Study Information
pubmed
1985
10.1016/0020-711x(85)90152-1