Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440
Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440
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DOI：
10.1002/1873-3468.12425
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发表时间：
2016-10-01
期刊：
影响因子：
3.5
通讯作者：
Nojiri, Hideaki
中科院分区：
文献类型：
--
作者：
Suzuki-Minakuchi, Chiho;Kawazuma, Kohei;Nojiri, Hideaki
H-NS 家族蛋白在细菌核仁压缩和整体转录中发挥着关键作用。假单胞菌中的 MvaT 同源物与 H-NS 的氨基酸序列同一性几乎可以忽略不计，但可以补充大肠杆菌的 hns 相关表型。在这里，我们报道了恶臭假单胞菌 KT2440 中 MvaT 同源物 TurB 的 N 端二聚/寡聚结构域的晶体结构。我们的数据确定了两个二聚位点；中心二聚位点的结构与H-NS的相应区域几乎相同，而末端二聚位点则不同。我们的结果揭示了 H-NS 和 TurB 之间二聚和寡聚机制的相似性和差异。
H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB.