When Too Much ATP Is Bad for Protein Synthesis.
When Too Much ATP Is Bad for Protein Synthesis.
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DOI：
10.1016/j.jmb.2015.06.021
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发表时间：
2015-08-14
影响因子：
5.6
通讯作者：
Groisman EA
中科院分区：
文献类型：
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作者：
Pontes MH;Sevostyanova A;Groisman EA
三磷酸腺苷（ATP）是活细胞的能量货币。尽管ATP为几乎所有的能量依赖性活动提供动力，但大多数细胞ATP通过tRNA氨酰化和GTP再生用于蛋白质合成。镁（Mg2+）是活细胞中最常见的二价阳离子，通过维持核糖体的结构、参与翻译起始的生物化学以及作为ATP的抗衡离子而在蛋白质合成中起着至关重要的作用。ATP水平的非生理性增加阻碍了经历Mg 2+限制的细胞的生长，因为ATP是细胞中最丰富的核苷酸三磷酸，并且Mg 2+也是细胞质膜稳定所需的，并且作为必需酶的辅因子。我们认为，生物体科普Mg2+的限制，降低ATP水平和核糖体的生产，从而重新分配Mg2+不可或缺的细胞过程。
Adenosine triphosphate (ATP) is the energy currency of living cells. Even though ATP powers virtually all energy-dependent activity, most cellular ATP is utilized in protein synthesis via tRNA aminoacylation and GTP regeneration. Magnesium (Mg2+), the most common divalent cation in living cells, plays crucial roles in protein synthesis by maintaining the structure of ribosomes, participating in the biochemistry of translation initiation and functioning as a counter-ion for ATP. A non-physiological increase in ATP levels hinders growth in cells experiencing Mg2+ limitation because ATP is the most abundant nucleotide triphosphate in the cell and Mg2+ is also required for the stabilization of the cytoplasmic membrane and as a cofactor for essential enzymes. We propose that organisms cope with Mg2+ limitation by decreasing ATP levels and ribosome production, thereby reallocating Mg2+ to indispensable cellular processes.