The N-terminal Acetyltransferase Naa10/ARD1 Does Not Acetylate Lysine Residues
The N-terminal Acetyltransferase Naa10/ARD1 Does Not Acetylate Lysine Residues
复制标题
DOI：
10.1074/jbc.m115.709428
复制
发表时间：
2016-03-04
影响因子：
4.8
通讯作者：
Marmorstein, Ronen
中科院分区：
文献类型：
--
作者：
Magin, Robert S.;March, Zachary M.;Marmorstein, Ronen
N-末端乙酰转移酶NatA是由催化亚基（Naa 10/ARD 1）和辅助亚基（Naa 15）组成的异二聚体复合物。NatA共乙酰化多种新生多肽的N末端。此外，Naa 10可以独立地作用于一组不同的底物，特别是肌动蛋白的后乙酰化。最近对Naa 10的结构研究也揭示了N末端乙酰化特异性的分子基础。令人惊讶的是，最近的报告声称，Naa 10也可以乙酰化赖氨酸残基的不同目标，包括蛋氨酸亚砜还原酶A，肌球蛋白轻链激酶，和Runt相关的转录因子2。在这里，我们使用重组蛋白质，以重建和评估赖氨酸乙酰化事件在体外催化Naa 10。我们发现，有或没有Naa 10的底物蛋白质的赖氨酸乙酰化没有差异，这表明底物可能是乙酰化的化学，而不是酶。总之，我们的数据反对Naa 10在赖氨酸乙酰化中的作用。
The N-terminal acetyltransferase NatA is a heterodimeric complex consisting of a catalytic subunit (Naa10/ARD1) and an auxiliary subunit (Naa15). NatA co-translationally acetylates the N termini of a wide variety of nascent polypeptides. In addition, Naa10 can act independently to posttranslationally acetylate a distinct set of substrates, notably actin. Recent structural studies of Naa10 have also revealed the molecular basis for N-terminal acetylation specificity. Surprisingly, recent reports claim that Naa10 may also acetylate lysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kinase, and Runt-related transcription factor 2. Here we used recombinant proteins to reconstitute and assess lysine acetylation events catalyzed by Naa10 in vitro. We show that there is no difference in lysine acetylation of substrate proteins with or without Naa10, suggesting that the substrates may be acetylated chemically rather than enzymatically. Together, our data argue against a role for Naa10 in lysine acetylation.