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

Anastacia R Parks, Jorge C Escalante-Semerena
{"title":"Protein N-terminal acylation: An emerging field in bacterial cell physiology.","authors":"Anastacia R Parks,&nbsp;Jorge C Escalante-Semerena","doi":"10.31300/ctmb.16.2022.1-18","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":72760,"journal":{"name":"Current trends in microbiology","volume":"16 ","pages":"1-18"},"PeriodicalIF":0.0000,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10062008/pdf/nihms-1878358.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current trends in microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.31300/ctmb.16.2022.1-18","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

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

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
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。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Protein N-terminal acylation: An emerging field in bacterial cell physiology. T cell responses to adenoviral vectors expressing the SARS-CoV-2 nucleoprotein. Management of methicillin-resistant Staphylococcus aureus mediated ventilator-associated pneumonia. New insights on the development of Streptomyces and their relationships with secondary metabolite production.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1