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首页> 外文期刊>Biochemistry >Characterizing the Structure and Oligomerization of Major Royal Jelly Protein 1 (MRJP1) by Mass Spectronietry and Complementary Biophysical Tools
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Characterizing the Structure and Oligomerization of Major Royal Jelly Protein 1 (MRJP1) by Mass Spectronietry and Complementary Biophysical Tools

机译：通过质谱和互补的生物物理工具表征主要蜂王浆蛋白 1 （MRJP1） 的结构和寡聚化

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摘要

Royal jelly (RJ) triggers the development of female honeybee MRJP1 larvae into queens. This effect has been attributed to the presence of major royal jelly protein 1 (MRJP1) in RJ. MRJP1 isolated from royal jelly is tightly associated with apisimin, a 54-residue alpha-helical peptide that promotes the noncovalent assembly of MRJP1 into multimers. No high-resolution structural data ate available for these complexes, and their binding stoichiometry, remains uncertain. We examined MRJP(1)/apisimin using a range of biophysical techniques. We also investigated the behavior of deglycosylated samples, as well as samples with reduced apisimin content, Our mass spectrometry (MS) data demonstrate that the native complexes predominantly exist in a (MRJP1(4) apisimin(4)) stoichiometry. Hydrogen/deuterium exchange MS reveals that MRJP1 within these complexes is extensively disordered in the range of residues 20-265. Marginally stable secondary structure (likely antiparallel beta-sheet) exists around residues 266-432. These weakly structured regions interchange with conformers that are extensively unfolded, giving rise to bimodal (EX1) isotope distributions; We propose that the native complexes have a "dimer of dimers" quaternary structure in which MRJP1 chains are bridged by apisimin. Specifically, our data suggest that apisimin acts as a linker that forms hydrophobic contacts involving the MRJP1 segment (316)VLFFGLV(322). Deglycosylation produces large soluble aggregates, highlighting the role of glycans as aggregation inhibitors. Samples with reduced apisimin content form dimeric complexes with a (MRJP1(2) apisimin(1)) stoichiometry. The information uncovered in this work will help pave the way toward a better understanding of the unique physiological role played by MRJP1 during queen differentiation.
机译：蜂王浆 （RJ） 触发雌性蜜蜂 MRJP1 幼虫发育成蜂王。这种效应归因于 RJ 中主要蜂王浆蛋白 1 （MRJP1） 的存在。从蜂王浆中分离出的 MRJP1 与 apisimin 紧密结合，apisimin 是一种 54 个残基的 α-螺旋肽，可促进 MRJP1 非共价组装成多聚体。这些复合物及其结合化学计量学尚不确定。我们使用一系列生物物理技术检查了 MRJP（1）/apisimin。我们还研究了去糖基化样品的行为，以及apisimin含量降低的样品，我们的质谱（MS）数据表明，天然复合物主要存在于（MRJP1（4）apisimin（4））化学计量中。氢/氘交换 MS 显示这些复合物中的 MRJP1 在残基 20-265 范围内广泛无序。残基 266-432 周围存在略微稳定的二级结构（可能是反平行 β-折叠）。这些弱结构区域与广泛展开的构象相互作用，产生双峰 （EX1） 同位素分布;我们提出天然复合物具有“二聚体二聚体”四级结构，其中 MRJP1 链被 apisimin 桥接。具体来说，我们的数据表明，apisimin 充当连接子，形成涉及 MRJP1 片段的疏水接触 （316）VLFFGLV（322）。去糖基化产生大的可溶性聚集体，突出了聚糖作为聚集抑制剂的作用。apisimin含量降低的样品通过（MRJP1（2）apisimin（1））化学计量形成二聚体复合物。这项工作中发现的信息将有助于为更好地理解MRJP1在蜂王分化过程中发挥的独特生理作用铺平道路。

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