研究人員在2月在線出版的《自然—化學(xué)生物學(xué)》(Nature Chemical Biology)期刊上報(bào)告說,,他們發(fā)明了一種新方法,,可以將乙酰基定點(diǎn)加入到蛋白質(zhì)中,。
乙?;且环N很小的化學(xué)物質(zhì),它被加入到細(xì)胞中各種各樣的蛋白質(zhì)上,,這對調(diào)節(jié)表觀遺傳過程和細(xì)胞信號過程來說都至關(guān)重要,。事實(shí)上,將乙?;拥降鞍踪|(zhì)上是如此普遍,,以至于它的重要性似乎可等同于控制細(xì)胞過程的磷酸化作用。然而,,科學(xué)家們對這種蛋白質(zhì)的乙?;饔玫臋C(jī)理知之甚少,因?yàn)楹茈y將乙?;尤氲降鞍踪|(zhì)的指定位置,從而研究它的作用,。
Jason Chin和同事發(fā)明了一種方法,,可將乙酰基加到埃希氏菌蛋白質(zhì)的指定位置,。這是一種簡單的蛋白質(zhì)乙?;椒ǎ璐朔椒?,研究人員能夠研究這一重要的生理學(xué)修飾,。(科學(xué)時(shí)報(bào) 王丹紅/編譯)
生物谷推薦原始出處:
(Nature Chemical Biology),doi:10.1038/nchembio.73,,Heinz Neumann,,Jason W Chin
Genetically encoding N-acetyllysine in recombinant proteins
Heinz Neumann1, Sew Y Peak-Chew1 & Jason W Chin1
N-acetylation of lysine (1) is a reversible post-translational modification with a regulatory role that rivals that of phosphorylation in eukaryotes. No general methods exist to synthesize proteins containing N-acetyllysine (2) at defined sites. Here we demonstrate the site-specific incorporation of N-acetyllysine in recombinant proteins produced in Escherichia coli via the evolution of an orthogonal N-acetyllysyl-tRNA synthetase/tRNACUA pair. This strategy should find wide applications in defining the cellular role of this modification.
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Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH England, UK.