Charged residues flanking aggregation‐prone regions play a role in protein folding and prevention of aggregation. In this issue of The EMBO Journal , Houben et al exploit the role of such charged gatekeepers in aggregation suppression and find that negative charges are more effective than positive ones. Strikingly, the prominent Hsp70 chaperone has a strong preference for the less effective, basic gate keepers. This implies co‐adaptation of chaperone specificity and composition of protein sequences in evolution.

中文翻译：

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在封闭的大门后面-分子伴侣和带电荷的残基决定了蛋白质的命运。

易聚集区域两侧的带电残基在蛋白质折叠和防止聚集中起作用。在本期《 EMBO Journal》中，Houben等人利用了带电看门人在抑制聚集中的作用，发现负电荷比正电荷更有效。令人惊讶的是，著名的Hsp70分子伴侣强烈反对效率较低的基本门卫。这意味着在进化中伴侣伴侣特异性和蛋白质序列组成的共同适应。