Venkat Sumana, Nannapaneni Dharma Theja, Gregory Caroline, Gan Qinglei, McIntosh Matt, Fan Chenguang
Department of Chemistry and Biochemistry University of Arkansas Fayetteville AR USA.
Department of Biological Sciences University of Arkansas Fayetteville AR USA.
FEBS Open Bio. 2017 Oct 16;7(11):1805-1814. doi: 10.1002/2211-5463.12320. eCollection 2017 Nov.
Reversible lysine acetylation is one of the most widely distributed post-translational modifications; it is involved in a variety of biological processes and can be found in all three domains of life. Acetyltransferases and deacetylases work coordinately to control levels of protein acetylation. In this work, we applied the genetic code expansion strategy to site-specifically incorporate -thioacetyl-l-lysine (TAcK) as an analog of -acetyl-l-lysine (AcK) into green fluorescent protein and malate dehydrogenase in . We showed that TAcK could serve as an ideal functional mimic for AcK. It could also resist the bacterial sirtuin-type deacetylase CobB. Thus, genetic incorporation of TAcK as a non-deacetylatable analog of AcK into proteins will facilitate studies of protein acetylation.
可逆赖氨酸乙酰化是分布最为广泛的翻译后修饰之一；它参与多种生物过程，并且在生命的三个域中均有发现。乙酰转移酶和去乙酰化酶协同作用以控制蛋白质乙酰化水平。在本研究中，我们应用遗传密码扩展策略，将硫代乙酰基-L-赖氨酸（TAcK）作为乙酰基-L-赖氨酸（AcK）的类似物位点特异性地掺入大肠杆菌中的绿色荧光蛋白和苹果酸脱氢酶中。我们表明，TAcK可作为AcK的理想功能模拟物。它还能抵抗细菌沉默调节蛋白型去乙酰化酶CobB。因此，将TAcK作为AcK的不可去乙酰化类似物遗传掺入蛋白质中将有助于蛋白质乙酰化的研究。
