Structural and nucleic acid binding properties of hepatitis delta virus small antigen.
Structural and nucleic acid binding properties of hepatitis delta virus small antigen.
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DOI：
10.5501/wjv.v6.i2.26
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发表时间：
2017-05-12
期刊：
影响因子：
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通讯作者：
Cunha, Celso
中科院分区：
文献类型：
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作者：
Alves, Carolina;Cheng, Hong;Cunha, Celso
目的：为了进一步表征 195 个氨基酸的小 δ 抗原 S-HDAg 的结构和核酸结合特性，对截短形式的 S-HDAg 进行了研究，其中包含氨基酸 61-195 (Δ60HDAg)，因此缺乏二聚化和高阶多聚化所必需的结构域。方法：使用圆二色性和核磁共振实验 评估 Δ60HDAg 的结构。通过凝胶阻滞测定研究了核酸结合特性。结果：结果显示截短的 Δ60HDAg 蛋白本质上是无序但紧凑的，而包含残基 94-146 的 RNA 结合域采用动态螺旋构象。我们还发现 Δ60HDAg 未能多聚化，但仍具有核酸结合活性，表明多聚化对于核酸结合不是必需的。此外，与之前报道的全长蛋白一致，截短蛋白在核酸结合方面没有发现明显的特异性。结论：综合这些结果可以得出结论：Δ60HDAg 本质上是无序但紧凑的； Δ60HDAg 不是多聚体，但仍然能够结合核酸，尽管没有明显的特异性。
AIM: To further characterize the structure and nucleic acid binding properties of the 195 amino acid small delta antigen, S-HDAg, a study was made of a truncated form of S-HDAg, comprising amino acids 61-195 (∆60HDAg), thus lacking the domain considered necessary for dimerization and higher order multimerization.METHODS: Circular dichroism, and nuclear magnetic resonance experiments were used to assess the structure of ∆60HDAg. Nucleic acid binding properties were investigated by gel retardation assays.RESULTS: Results showed that the truncated ∆60HDAg protein is intrinsically disordered but compact, whereas the RNA binding domain, comprising residues 94-146, adopts a dynamic helical conformation. We also found that ∆60HDAg fails to multimerize but still contains nucleic acid binding activity, indicating that multimerization is not essential for nucleic acid binding. Moreover, in agreement with what has been previously reported for full-length protein, no apparent specificity was found for the truncated protein regarding nucleic acid binding.CONCLUSION: Taken together these results allowed concluding that ∆60HDAg is intrinsically disordered but compact; ∆60HDAg is not a multimer but is still capable of nucleic acid binding albeit without apparent specificity.