二聚体亲和素自组装成独特的高阶寡聚物,The FEBS Journal

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二聚体亲和素自组装成独特的高阶寡聚物
The FEBS Journal ( IF 5.5 ) Pub Date : 2023-02-28 , DOI: 10.1111/febs.16764
Juana Bana ₁ , Jessica Warwar ₁ , Edward A Bayer _{2,

3} , Oded Livnah ₁

Affiliation

近年来，二聚体亲和素家族不断扩大，包含了许多新成员。它们都缺乏在生物素结合中起关键作用的单体间色氨酸。尽管如此，抗生物素蛋白的这些新成员仍保持对生物素的高亲和力。此外，所有二聚体亲和素都有一个非常独特的特性：即晶体结构中的圆柱形寡聚。这里描述的最新成员是来自农杆菌根瘤菌的农杆菌亲和素。AAP43具有相同的重要结构特征。然而，农杆菌亲和素对生物素的亲和力低于亲和素家族的所有其他成员，因为生物素结合位点中存在苯丙氨酸而不是保守的酪氨酸。将这种苯丙氨酸突变为酪氨酸重新产生了高亲和力，这强调了这种特殊酪氨酸残基的重要性。农业亲和素与其他二聚体亲和素的另一个独特特征是它的晶体结构中不产生寡聚物。为了了解促进二聚亲和素寡聚化的因素，我们将农杆菌亲和素的 C 末端区域与产生八聚体的 Hoefavidin 的 C 末端区域交换。这种交换产生了十聚体而不是八聚体。这一不寻常的结果证明了 C 末端区域对产生寡聚物的能力的影响。农杆菌亲和素的十聚体组装进一步扩展了亲和素-生物素工具箱，并且很可能为基于生物素的新技术铺平道路。此外，揭示诱导二聚抗生物素蛋白形成寡聚组装体的因素可能有助于更好地理解促进寡聚化的一般分子决定因素。

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Self-assembly of a dimeric avidin into unique higher-order oligomers

The dimeric avidin family has been expanded in recent years to include many new members. All of them lack the intermonomeric Trp that plays a critical role in biotin-binding. Nevertheless, these new members of the avidins maintain the high affinity towards biotin. Additionally, all of the dimeric avidins share a very unique property: namely, the cylindrical oligomerization in the crystal structure. The newest member described here, agroavidin from the agrobacterium, Rhizobium sp. AAP43, shares their important structural features. However, the affinity of agroavidin towards biotin is lower than all other members of the avidin family, due to the presence of phenylalanine instead of a conserved tyrosine in the biotin-binding site. Mutating this phenylalanine into tyrosine regenerated the high affinity, which emphasizes the importance of this particular tyrosine residue. Another unique feature that distinguishes agroavidin from the other dimeric avidins is that it does not produce oligomers in its crystal structure. In order to understand the factors that promote oligomerization in dimeric avidins, we exchanged the C-terminal region of agroavidin with that of hoefavidin that produced octamers. This exchange resulted in a decamer rather than an octamer. This unusual outcome demonstrates the impact of the C-terminal region on the ability to produce oligomers. The decameric assembly of agroavidin expands the avidin-biotin toolbox even further and could well pave the path into new biotin-based technologies. Moreover, uncovering the factors that induce dimeric avidins into oligomeric assemblies may aid in better understanding the general molecular determinants that promote oligomerization.

更新日期：2023-02-28

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