DNA-Binding Properties of YbaB, a Putative Nucleoid-Associated Protein From Caulobacter crescentus.

DNA-Binding Properties of YbaB, a Putative Nucleoid-Associated Protein From Caulobacter crescentus.
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DOI:
10.3389/fmicb.2021.733344
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发表时间:
2021
影响因子:
5.2
通讯作者:
Priyadarshini R
Priyadarshini R
中科院分区:
生物学2区
文献类型:
--
作者:
Pal P;Modi M;Ravichandran S;Yennamalli RM;Priyadarshini R

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类核相关蛋白(NAPs)或组蛋白样蛋白(HLPs)是存在于细菌中的DNA结合蛋白,在类核结构和基因调控中起重要作用。NAP通过DNA弯曲、桥接或形成聚集体来影响细菌类核组织。EbfC是首先在伯氏疏螺旋体中鉴定的类核蛋白,属于能够结合和改变DNA构象的NAPs的YbaB/EbfC家族。在大肠杆菌和流感嗜血杆菌中发现的EbfC的直系同源物YbaB也充当转录调节因子。YbaB具有一种新的镊子状结构,并以同源二聚体的形式结合DNA。YbaB的同源物在几乎所有的细菌物种中被发现,这表明YbaB蛋白具有保守的功能,但YbaB蛋白在许多细菌中的生理作用还不清楚。在这项研究中,我们的特点YbaB/EbfC家族DNA结合蛋白的新月柄杆菌。C. crescentus具有一个在基因组中注释的YbaB/EbfC家族基因(YbaBCc),并且它与YbaB/EbfC家族NAP共享41%的序列同一性。计算模型揭示了YbaBCc的镊子状结构,这是YbaB/EbfC家族NAP的特征。N-末端-CFP标记的YbaBCc定位于类核并且能够压缩DNA。不像B。YbaBCc蛋白是一种非特异性的DNA结合蛋白。crescentus。此外,YbaBCc保护DNA免受酶降解。总的来说,我们的研究结果表明,YbaBCc是一个小的组蛋白样蛋白,并可能在细菌染色体结构和基因调控中发挥作用。crescentus。
Nucleoid-associated proteins (NAPs) or histone-like proteins (HLPs) are DNA-binding proteins present in bacteria that play an important role in nucleoid architecture and gene regulation. NAPs affect bacterial nucleoid organization via DNA bending, bridging, or forming aggregates. EbfC is a nucleoid-associated protein identified first in Borrelia burgdorferi, belonging to YbaB/EbfC family of NAPs capable of binding and altering DNA conformation. YbaB, an ortholog of EbfC found in Escherichia coli and Haemophilus influenzae, also acts as a transcriptional regulator. YbaB has a novel tweezer-like structure and binds DNA as homodimers. The homologs of YbaB are found in almost all bacterial species, suggesting a conserved function, yet the physiological role of YbaB protein in many bacteria is not well understood. In this study, we characterized the YbaB/EbfC family DNA-binding protein in Caulobacter crescentus. C. crescentus has one YbaB/EbfC family gene annotated in the genome (YbaBCc) and it shares 41% sequence identity with YbaB/EbfC family NAPs. Computational modeling revealed tweezer-like structure of YbaBCc, a characteristic of YbaB/EbfC family of NAPs. N-terminal–CFP tagged YbaBCc localized with the nucleoid and is able to compact DNA. Unlike B. burgdorferi EbfC protein, YbaBCc protein is a non-specific DNA-binding protein in C. crescentus. Moreover, YbaBCc shields DNA against enzymatic degradation. Collectively, our findings reveal that YbaBCc is a small histone-like protein and may play a role in bacterial chromosome structuring and gene regulation in C. crescentus.
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