Addressing the Possibility of a Histone-Like Code in Bacteria.
Addressing the Possibility of a Histone-Like Code in Bacteria.
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DOI：
10.1021/acs.jproteome.0c00442
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发表时间：
2021-01-01
影响因子：
4.4
通讯作者：
Carabetta VJ
中科院分区：
文献类型：
--
作者：
Carabetta VJ
乙酰化最初是在20世纪60年代作为真核生物组蛋白的非结构化的、高度碱性的N-末端尾部的翻译后修饰（PTM）而被发现的。组蛋白乙酰化构成“组蛋白密码”的一部分，其调节染色体压实和各种DNA过程，例如基因表达、重组和DNA复制。在细菌中，核相关蛋白（NAPs）负责这些功能，因为它们组织和压缩染色体并调节一些DNA过程。高度保守的DNABII蛋白家族被认为是真核组蛋白的功能同源物，尽管没有序列或结构保守性。在过去的十年中，对Nε-赖氨酸乙酰化的兴趣日益增长，导致发现数百种细菌蛋白质被乙酰化，具有不同的细胞功能，这与最初认为这是一种罕见的现象形成鲜明对比。类似地，其他以前未发现的细菌PTM，如丝氨酸，苏氨酸和酪氨酸磷酸化，也已被表征。在这篇综述中，各种PTM之间发现DNABII家族蛋白质，特别是组蛋白样蛋白（HU）的直系同源物，从大规模的蛋白质组学研究进行了讨论。这些修改和酶的功能意义也得到了解决。在这些蛋白质上发现新的PTM引出了这个问题：细菌中是否存在组蛋白样密码？
Acetylation was initially discovered as a post-translational modification (PTM) on the unstructured, highly basic N-terminal tails of eukaryotic histones in the 1960s. Histone acetylation constitutes part of the “histone code”, which regulates chromosome compaction and various DNA processes such as gene expression, recombination, and DNA replication. In bacteria, nucleoid-associated proteins (NAPs) are responsible these functions in that they organize and compact the chromosome and regulate some DNA processes. The highly conserved DNABII family of proteins are considered functional homologues of eukaryotic histones despite having no sequence or structural conservation. Within the past decade, a growing interest in Nε-lysine acetylation led to the discovery that hundreds of bacterial proteins are acetylated with diverse cellular functions, in direct contrast to the original thought that this was a rare phenomenon. Similarly, other previously undiscovered bacterial PTMs, like serine, threonine, and tyrosine phosphorylation, have also been characterized. In this review, the various PTMs that were discovered among DNABII family proteins, specifically histone-like protein (HU) orthologues, from large-scale proteomic studies are discussed. The functional significance of these modifications and the enzymes involved are also addressed. The discovery of novel PTMs on these proteins begs this question: is there a histone-like code in bacteria?
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影响因子：
16.6
作者：
Bhowmick, Tuhin;Ghosh, Soumitra;Nagaraja, Valakunja
通讯作者：
Nagaraja, Valakunja
新型组蛋白翻译后修饰的蛋白质组学表征。
影响因子：
3.9
作者：
Arnaudo AM;Garcia BA
通讯作者：
Garcia BA
DOI：
10.1073/pnas.51.5.786
发表时间：
1964-01-01
影响因子：
11.1
作者：
ALLFREY, VG;FAULKNER, R;MIRSKY, AE
通讯作者：
MIRSKY, AE
影响因子：
3.6
作者：
Crosby HA;Heiniger EK;Harwood CS;Escalante-Semerena JC
通讯作者：
Escalante-Semerena JC
影响因子：
5.6
作者：
BROYLES, SS;PETTIJOHN, DE
通讯作者：
PETTIJOHN, DE