A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1
A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1
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DOI：
10.1074/jbc.m211729200
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发表时间：
2003-03-07
影响因子：
4.8
通讯作者：
Matsunaga, T
中科院分区：
文献类型：
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作者：
Arakaki, A;Webb, J;Matsunaga, T
磁性细菌合成具有物种依赖性形态的磁铁矿晶体。控制纳米级磁铁矿晶体形成和不同形态生成的分子机制尚不清楚。通过对磁铁矿晶体相关蛋白的分析，从磁性螺菌菌株AMB-1中获得了几种与细菌磁铁矿紧密结合的低分子量蛋白。这些蛋白质在其氨基酸序列中显示出共同特征，其中包含疏水性 N 末端和亲水性 C 末端区域。 Mms5、Mms6、Mms7 和 Mms13 中的 G 末端区域含有密集的羧基和羟基，可结合铁离子。在酸性蛋白 Mms6 的存在下，通过化学合成磁铁矿，制备了与磁性细菌中类似的纳米尺寸磁性颗粒。这些蛋白质可能直接参与磁性细菌中生物磁铁矿晶体的形成。
Magnetic bacteria synthesize magnetite crystals with species-dependent morphologies. The molecular mechanisms that control nano-sized magnetite crystal formation and the generation of diverse morphologies are not well understood. From the analysis of magnetite crystal-associated proteins, several low molecular mass proteins tightly bound to bacterial magnetite were obtained from Magnetospirillum magneticum strain AMB-1. These proteins showed common features in their amino acid sequences, which contain hydrophobic N-terminal and hydrophilic C-terminal regions. The G terminal regions in Mms5, Mms6, Mms7, and Mms13 contain dense carboxyl and hydroxyl groups that bind iron ions. Nano-sized magnetic particles similar to those in magnetic bacteria were prepared by chemical synthesis of magnetite in the presence of the acidic protein Mms6. These proteins may be directly involved in biological magnetite crystal formation in magnetic bacteria.