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The generally good performance on such small bacterial genomes is encouraging, especially as it does not rely on the use of posttranslational modification and localization predictions, which are very informative features for eukaryotic proteins [ 13- 15].
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The role of posttranslational modification, such as reversible phosphorylation, remains unknown.
We have also focused on the role of posttranslational modifications in cohesin biology.
Furthermore, to our knowledge this study is the first successful example of studying protein lipidation, and one of only a few reports of posttranslational modification, in vivo using a metabolic chemical tagging approach, combined with bioorthogonal ligation reaction in a living organism.
Overall, this work demonstrates how the modularity of posttranslational modification enzymes can be used to design and synthesize desirable peptide motifs.
Additional levels of control include allosteric regulation, reversible phosphorylation, and other forms of posttranslational modification.
A key mechanism of posttranslational modification is ubiquitination by the ubiquitin-proteasome system (UPS).
Unfortunately, inactive enzyme could not be employed for the studies of posttranslational modification by proteolytic cleavage.
However, the impact of posttranslational modification on VHL nuclear and cytoplasmic localization still remains unclear.
O-GlcNAcylation of proteins is a common type of posttranslational modification.
GPI-anchoring is a form of posttranslational modification occurring in all eukaryotic cells [ 49].
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