Functions and mechanisms of protein lysine butyrylation (Kbu): Therapeutic implications in human diseases

Xue, Qianqian; Yang, Yanyan; Li, Hong; Li, Xiaoxin; Zou, Lu; Li, Tianxiang; Ma, Huibo; Qi, Hongzhao; Wang, Jianxun; Yu, Tao

doi:10.1016/j.gendis.2022.10.025

Cited by 6 publications

(1 citation statement)

References 95 publications

(111 reference statements)

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“…215 Lysine butyrylation exists in histones and is involved in the onset and progression of cancer, diabetes, and cardiovascular diseases as well as growth, development, and metabolism of rice. 216,217 OTSs for genetic encoding butyryl-lysine into proteins have been established in E. coli cells with WT MmPylRS 214 or MbPylRS. 215 Lysine crotonylation can be found in both histones and nonhistone proteins.…”

Section: Lysine Acylationmentioning

confidence: 99%

Orthogonal Translation for Site-Specific Installation of Post-translational Modifications

Gan,

Fan

2024

Chem. Rev.

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Post-translational modifications (PTMs) endow proteins with new properties to respond to environmental changes or growth needs. With the development of advanced proteomics techniques, hundreds of distinct types of PTMs have been observed in a wide range of proteins from bacteria, archaea, and eukarya. To identify the roles of these PTMs, scientists have applied various approaches. However, high dynamics, low stoichiometry, and crosstalk between PTMs make it almost impossible to obtain homogeneously modified proteins for characterization of the site-specific effect of individual PTM on target proteins. To solve this problem, the genetic code expansion (GCE) strategy has been introduced into the field of PTM studies. Instead of modifying proteins after translation, GCE incorporates modified amino acids into proteins during translation, thus generating site-specifically modified proteins at target positions. In this review, we summarize the development of GCE systems for orthogonal translation for site-specific installation of PTMs.

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