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Some types of post-translational modification are consequences of oxidative stress. Carbonylation is one example that targets the modified protein for degradation and can result in the formation of protein aggregates. [4] [5] Specific amino acid modifications can be used as biomarkers indicating oxidative damage. [6]
RiPPs consist of any peptides (i.e. molecular weight below 10 kDa) that are ribosomally-produced and undergo some degree of enzymatic post-translational modification.This combination of peptide translation and modification is referred to as "post-ribosomal peptide synthesis" (PRPS) in analogy with nonribosomal peptide synthesis (NRPS).
Post-translational modification is the chemical modification of a protein after its translation. It is one of the later steps in protein biosynthesis for many proteins.
Post-translational modifications can incorporate more complex, large molecules into the folded protein structure. One common example of this is glycosylation , the addition of a polysaccharide molecule, which is widely considered to be most common post-translational modification.
Transcriptional modification or co-transcriptional modification is a set of biological processes common to most eukaryotic cells by which an RNA primary transcript is chemically altered following transcription from a gene to produce a mature, functional RNA molecule that can then leave the nucleus and perform any of a variety of different functions in the cell. [1]
Acetylation is an important modification of proteins in cell biology; and proteomics studies have identified thousands of acetylated mammalian proteins. [1] [2] [3] Acetylation occurs as a co-translational and post-translational modification of proteins, for example, histones, p53, and tubulins.
Example of posttranslational modification detected on a 2D gel (spot boundaries delimited by analysis software, identification by mass spectrometry, P46462 is the protein ID in Expasy) Post-translational modification (PTM) isoforms are easily detected on 2D gels. Indeed, phosphorylation replaces neutral hydroxyl groups on serines, threonines ...
Protein phosphorylation is the most abundant post-translational modification in eukaryotes. Phosphorylation can occur on serine , threonine and tyrosine side chains (in other words, on their residues) through phosphoester bond formation, on histidine , lysine and arginine through phosphoramidate bonds , and on aspartic acid and glutamic acid ...