mRNA Engineering For Elongated Storage-shelf-life

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The half-life can be altered by mutations in the coding region of the mRNAs for c-fos, c-myc, and tubulin. Additionally, the stability of mRNAs and their half-lives are influenced by sequences that contain protein-binding sites.

Controlling the number of cellular transcripts and, in turn, the amounts of protein production requires regulation of mRNA turnover in the cytoplasm. mRNAs have a wide range of stability under a certain physiological environment. Controlling the number of cellular transcripts and, in turn, the amounts of protein production requires regulation of mRNA turnover in the cytoplasm. mRNAs have a wide range of stability under a certain physiological environment.

By observing alterations in the steady-state level of messenger RNA in the cytoplasm, messenger RNA stability is frequently indirectly examined. However, modifications to mRNA stability may not always result in changes in mRNA quantity. The half-lives of many mRNAs vary tenfold or more in response to cytokines, hormones, starvation, hypoxia, or viral infection. 

◆ The half-life of an mRNA can also be determined by its coding region.

◆ Half-lives of truncated mRNAs with most of their 3'-UTRs missing range from one to two hours.

◆ mRNAs become unstable when nonsense mutations are introduced in the 5'-part of the coding sequence.

Despite the innate stability that each mRNA has under certain circumstances, each mRNA's stability might fluctuate in response to a range of external stimuli. Controlling gene expression during the cell cycle, cell differentiation, immune response, as well as many other physiologic changes, is made possible by modulating mRNA stability.

Factors affecting the half-life of messenger RNA

Histone mRNA 3’-terminal stem-loop

The processing speeds at which the RNA in the nucleus is transported, translated, and destroyed are influenced by the 3'-UTRs of histone mRNAs lacking poly(A). These mRNAs are managed by the cell cycle. Only in cells in the S-phase do high quantities of histone mRNA (mRNA) accumulates. At the end of the S phase or when DNA replication is suppressed in S-phase cells, mRNAs are rapidly broken down. Histone mRNAs have a cis-element at the 3' end that controls how quickly they degrade.

AU-rich elements (AUREs): 

mRNAs with an oligo(U) or AURE region at the 3'-UTR are more likely to be unstable. The chimeric transcript decays with a half-life of fewer than 30 minutes when an AURE from the 39-UTR of an unstable mRNA is inserted into the 39-UTR of an mRNA expressing granulocyte-macrophage colony-stimulating factor (GM-CSF). RNA stability in mammalian cells is controlled by ARUEs. For instance, the AUUUA sequences speed up the mRNA body's decomposition.

Iron-responsive element (IRE)

Depending on the level of intracellular iron, the mRNAs that encode the transferrin receptor and ferritin are controlled post-transcriptionally. Iron is taken in by cells through the transferrin receptor. A significant protein that stores iron in cells is ferritin. 

It appears that the main non-specific mRNA-binding protein that forms mRNPs and is a member of the unique p50 family of basic, glycine-rich, phosphorylatable proteins is necessary but insufficient for the masking. The 3′-untranslated regions' (3′-UTR) interactions with sequence-specific proteins appear to be crucial for the masking of mRNPs.

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