Protein N-terminal acylation: An emerging field in bacterial cell physiology.

Anastacia R Parks, Jorge C Escalante-Semerena
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Abstract

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.

Abstract Image

Abstract Image

蛋白质n端酰化:细菌细胞生理学的新兴领域。
n端酰基化是指在肽链末端α氨基上不可逆地增加酰基部分。这种类型的修饰改变了N端的性质,可以通过破坏蛋白质的相互作用、功能、定位、降解、疏水性或电荷来干扰修饰蛋白的功能。Nt酰化存在于生命的所有领域,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,除核糖体蛋白外,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认识到的更为常见。本文就原核细胞中Nt乙酰化的研究进展、相关乙酰基转移酶的研究进展以及目前研究Nt乙酰化的方法进行了综述。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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