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首页> 外文期刊>The FEBS journal >Light-induced complex formation of bacteriophytochrome RpBphP1 and gene repressor RpPpsR2 probed by SAXS
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Light-induced complex formation of bacteriophytochrome RpBphP1 and gene repressor RpPpsR2 probed by SAXS

机译：通过撒克塞探测的光学诱导的噬菌体rpbph1和基因抑制仪的基因抑制仪的复杂形成

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摘要

Bacteriophytochrome proteins (BphPs) are molecular light switches that enable organisms to adapt to changing light conditions through the control of gene expression. Canonical type 1 BphPs have histidine kinase output domains, but type 3 RpBphP1, in the bacterium Rhodopseudomonas palustris (Rps. palustris), has a C terminal PAS9 domain and a two-helix output sensor (HOS) domain. Type 1 BphPs form head-to-head parallel dimers; however, the crystal structure of RpBphP1 Delta HOS, which does not contain the HOS domain, revealed pseudo anti-parallel dimers. HOS domains are homologs of Dhp dimerization domains in type 1 BphPs. We show, by applying the small angle X-ray scattering (SAXS) technique on full-length RpBphP1, that HOS domains fulfill a similar role in the formation of parallel dimers. On illumination with far-red light, RpBphP1 forms a complex with gene repressor RpPpsR2 through light-induced structural changes in its HOS domains. An RpBphP1:RpPpsR2 complex is formed in the molecular ratio of 2 : 1 such that one RpBphP1 dimer binds one RpPpsR2 monomer. Molecular dimers have been modeled with Pfr and Pr SAXS data, suggesting that, in the Pfr state, stable dimeric four alpha-helix bundles are formed between HOS domains, rendering RpBphP1functionally inert. On illumination with light of 760 nm wavelength, four alpha-helix bundles formed by HOS dimers are disrupted, rendering helices available for binding with RpPpsR2.
机译：噬菌体蛋白质（BPHPS）是分子光开关，使生物能够通过控制基因表达来适应变化的光源。规范类型1 BphPs具有组氨酸激酶输出域，但3型RpBphP1，在细菌沼泽红假单胞菌（RPS。沼泽），具有C末端PAS9结构域和两螺旋输出传感器（HOS）结构域。 1型BPHPS形成头部到头平行二聚体;然而，RPBPHP1ΔHOS的晶体结构，其不含HOS结构域，揭示了伪抗平行二聚体。 HOS结构域是1 BPHPS中的DHP二聚化结构域的同源物。我们通过将小角度X射线散射（SAXS）技术应用于全长RPBPHP1，HOS结构域在平行二聚体的形成中满足了类似的作用。在具有远红光的照明中，RPBPHP1通过其HOS结构域的光诱导的结构变化与基因抑制仪RPPPSR2形成复合物。 RPBPHP1：RPPPSR2复合物以2：1的分子比形成，使得一个RPBPP1二聚体结合一种RPPPSR2单体。分子二聚体已经用PFR和PR SAXS数据进行建模，表明，在PFR状态下，在HOS结构域之间形成稳定的二聚体四个α-螺旋束，呈现RPBPHP1功能惰性。在具有760nm波长的光的照明中，Hos二聚体形成的四个α-螺旋束被破坏，渲染可用于与RPPPSR2结合的螺旋。

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