Protein N-terminal acylation: An emerging field in bacterial cell physiology.
Protein N-terminal acylation: An emerging field in bacterial cell physiology.
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DOI：
10.31300/ctmb.16.2022.1-18
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发表时间：
2022
期刊：
影响因子：
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通讯作者：
Escalante-Semerena, Jorge C
中科院分区：
文献类型：
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作者：
Parks, Anastacia R;Escalante-Semerena, Jorge C
N-末端（Nt）-酰化是将酰基部分不可逆地添加到肽链的末端α氨基。这种类型的修饰改变了N末端的性质，这可以通过破坏蛋白质相互作用、功能、定位、降解、疏水性或电荷来干扰修饰蛋白质的功能。Nt酰化存在于生命的所有领域，并且在真核细胞中非常常见。然而，在原核生物中很少有Nt酰化的报道。人们曾经认为，除了核糖体蛋白之外，蛋白质的Nt酰化在原核生物中并不常见，但最近的证据表明，这种修饰可能比以前意识到的更常见。在这篇综述中，我们讨论了什么是已知的原核Nt乙酰化和乙酰转移酶负责，以及在这一领域的最新进展和目前使用的方法来研究Nt乙酰化。
N-terminal (Nt)-acylation is the irreversible addition of an acyl moiety to the terminal alpha amino group of a peptide chain. This type of modification alters the nature of the N terminus, which can interfere with the function of the modified protein by disrupting protein interactions, function, localization, degradation, hydrophobicity, or charge. Nt acylation is found in all domains of life and is a highly common occurrence in eukaryotic cells. However, in prokaryotes very few cases of Nt acylation have been reported. It was once thought that Nt acylation of proteins, other than ribosomal proteins, was uncommon in prokaryotes, but recent evidence suggests that this modification may be more common than once realized. In this review, we discuss what is known about prokaryotic Nt acetylation and the acetyltransferases that are responsible, as well as recent advancements in this field and currently used methods to study Nt acetylation.