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Review
. 2016 Feb 29:10:861-71.
doi: 10.2147/DDDT.S80496. eCollection 2016.

The interplay of post-translational modification and gene therapy

Victor Chukwudi Osamor  1 , Shalom N Chinedu  2 , Dominic E Azuh  3 , Emeka Joshua Iweala  2 , Olubanke Olujoke Ogunlana  2
Affiliations
Review

The interplay of post-translational modification and gene therapy

Victor Chukwudi Osamor et al. Drug Des Devel Ther. .

Abstract

Several proteins interact either to activate or repress the expression of other genes during transcription. Based on the impact of these activities, the proteins can be classified into readers, modifier writers, and modifier erasers depending on whether histone marks are read, added, or removed, respectively, from a specific amino acid. Transcription is controlled by dynamic epigenetic marks with serious health implications in certain complex diseases, whose understanding may be useful in gene therapy. This work highlights traditional and current advances in post-translational modifications with relevance to gene therapy delivery. We report that enhanced understanding of epigenetic machinery provides clues to functional implication of certain genes/gene products and may facilitate transition toward revision of our clinical treatment procedure with effective fortification of gene therapy delivery.

Keywords: epigenetics; gene therapy; histone; methylation; post-translational modification.

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Figures

Figure 1
Figure 1
Mutagenic deamination of DNA methylation. Notes: This process started originally with an epigenetic change of cytosine during methylation, but a resultant deamination of an intermediate product (5-methyl cytosine) made it a complicated situation beyond epigenetics, to a possible SNP. This is therefore not strictly an epigenetic change, notwithstanding that it started like usual DNA methylation. Abbreviation: SNP, single nucleotide polymorphism.
Figure 2
Figure 2
Nucleosome and component histones. Notes: The octamer histone core (H2A, H2B, H3, and H4) is wrapped by the DNA and locked on the outside by H1 histone.
Figure 3
Figure 3
Chemical structures of major histone modifications. Notes: The chemical structure represents the histone marks for some lysine and arginine amino acid modifications. They are formed by covalent addition of either acetyl or methyl groups or their multiples.
Figure 4
Figure 4
The cis and trans isomers of proline. Notes: The process of the formation of trans and cis conformation is via isomerism, and the reaction is a reversible process.
See this image and copyright information in PMC

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