Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways.
Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways.
复制标题
DOI：
10.1098/rsif.2022.0391
复制
发表时间：
2022-08
期刊：
影响因子：
--
通讯作者：
中科院分区：
文献类型：
--
作者：
磷酸盐和硫酸盐基团是能量代谢的组成部分，并将负电荷引入生物大分子。这种修饰的一个目的是诱导蛋白质伙伴的精确结合/激活。这两个基团的物理化学性质虽然表面上相似，但在一个重要的方面不同-中心(磷或硫)原子的价态。这决定了它们各自的酯和双酯的不同性质，从而决定了它们的电荷、与金属离子的相互作用以及它们的溶解性。这些反过来又决定了每个群体在生物系统中进化的不同角色。这两种修饰之间存在生物合成联系；硫酸盐供体3‘-磷酸腺苷-5’-磷酸硫酸盐由三磷酸腺苷(ATP)和腺苷磷酸硫酸盐形成，而后者由硫酸盐阴离子和ATP生成。此外，连接新生糖胺聚糖(GAG)链和其亲本蛋白多糖的四糖连接区的木糖残基被木糖基激酶(FAM20B，糖胺聚糖木糖基酶)磷酸化，大大加速了它们的生物合成。根据观察到的Gag链可以进入细胞核，假设硫酸化GAG可以影响细胞核中的事件，这将通过复杂、相互连接的信号网络完成一个反馈环，将磷酸化和硫化的互补阴离子修饰结合在一起，值得进一步研究。
Phosphate and sulfate groups are integral to energy metabolism and introduce negative charges into biological macromolecules. One purpose of such modifications is to elicit precise binding/activation of protein partners. The physico-chemical properties of the two groups, while superficially similar, differ in one important respect—the valency of the central (phosphorus or sulfur) atom. This dictates the distinct properties of their respective esters, di-esters and hence their charges, interactions with metal ions and their solubility. These, in turn, determine the contrasting roles for which each group has evolved in biological systems. Biosynthetic links exist between the two modifications; the sulfate donor 3′-phosphoadenosine-5′-phosphosulfate being formed from adenosine triphosphate (ATP) and adenosine phosphosulfate, while the latter is generated from sulfate anions and ATP. Furthermore, phosphorylation, by a xylosyl kinase (Fam20B, glycosaminoglycan xylosylkinase) of the xylose residue of the tetrasaccharide linker region that connects nascent glycosaminoglycan (GAG) chains to their parent proteoglycans, substantially accelerates their biosynthesis. Following observations that GAG chains can enter the cell nucleus, it is hypothesized that sulfated GAGs could influence events in the nucleus, which would complete a feedback loop uniting the complementary anionic modifications of phosphorylation and sulfation through complex, inter-connected signalling networks and warrants further exploration.
登录
查看更多内容
影响因子：
3.3
作者：
Andreev, Marat;Chremos, Alexandros;Douglas, Jack F.
通讯作者：
Douglas, Jack F.
DOI：
10.1016/j.bbrc.2009.10.107
发表时间：
2009-12-25
影响因子：
3.1
作者：
Bostrom, S. Lynn;Dore, Justin;Griffith, Leslie C.
通讯作者：
Griffith, Leslie C.
影响因子：
3.3
作者：
Andreev, Marat;de Pablo, Juan J.;Douglas, Jack F.
通讯作者：
Douglas, Jack F.
影响因子：
21.3
作者：
Cohen, P
通讯作者：
Cohen, P
影响因子：
4.8
作者：
Guerrini, Marco;Guglieri, Sara;Viskov, Christian
通讯作者：
Viskov, Christian