利用基于saxs的解离试验表征结核分枝杆菌中dna - dnag相互作用。

IF 2.6 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

ChemBioChem Pub Date : 2025-06-11 DOI:10.1002/cbic.202500289

Barak Akabayov, Adi Dayan, Stefan Ilic

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引用次数: 0

摘要

我们研究了解旋酶和引物酶之间的复杂相互作用，这是参与结核分枝杆菌DNA复制的复制体的两个关键成分。利用这些蛋白质纯化的互补结构域，我们采用表面等离子体共振（SPR）分析和交联分析来表征它们的结合动力学。SPR分析显示，结合解离常数为0.21±0.08µM，交联实验表明可能形成异二聚体。重要的是，我们利用小角度x射线散射（SAXS）解离实验来研究溶液中蛋白质之间的动态相互作用。我们的发现通过揭示解旋酶和引物酶之间的结构相互作用，为针对结核分枝杆菌DNA复制的靶向治疗策略提供了新的机会。

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Characterization of DnaB-DnaG Interaction in M. tuberculosis using a SAXS-Based Dissociation Assay.

We studied the complex interactions between helicase and primase, two key components of the replisome involved in DNA replication in Mycobacterium tuberculosis. Utilizing purified, complementary domains of these proteins, we employed a surface plasmon resonance (SPR) analysis and a cross-linking assay to characterize their binding dynamics. The SPR analysis revealed a binding dissociation constant of 0.21 ± 0.08 µM, and the cross-linking assay suggested the possible formation of a heterodimer species. Importantly, we utilized a small-angle X-ray scattering (SAXS) dissociation assay to study the dynamic interactions between the proteins in solution. Our findings provide new opportunities for targeted therapeutic strategies aimed at DNA replication in M. tuberculosis by revealing the structural interplay between helicase and primase.

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来源期刊

ChemBioChem 生物-生化与分子生物学

CiteScore

6.10

自引率

3.10%

发文量

407

审稿时长

1 months

期刊介绍： ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).