S-(1,2,3,4-四氢-2-羟基-1-萘基)-L-半胱氨酸掺入蛋白质的机制。
Mechanism for the incorporation of S-(1,2,3,4-tetrahydro-2-hydroxy-1-naphthyl)-L-cysteine into protein.
作者信息
Morrison W C, Whybrew W D, Sobhy C M, Morrison J C, Trass T C, Bucovaz E T
出版信息
Br J Cancer. 1977 Feb;35(2):218-25. doi: 10.1038/bjc.1977.29.
Evidence is presented which indicates that S-(1,2,3,4-tetrahydro-2-hydroxy-1-naphthyl)-L-cysteine (THN-cysteine), formed by the reaction of 1,2-epoxy-THN with cysteine, can be incorporated into protein; The position of incorporation of THN-cysteine into protein would depend on whether the epoxide of THN reacts with cysteinyl-tRNACyS or with cysteine. In both cases, the mechanism of incorporation of THN-cysteine into protein is the same as for the natural amino acids. For example, the incorporation of THN-cysteinyl-tRNACyS is stimulated by Poly-UG, the code for tRNACyS, and would be expected to be substituted for cysteine in protein being synthesized, whereas THN-cysteine not previously esterified to tRNA is activated by the isoleucyl- and valyl-RNA synthetases, and its incorporation is stimulated by Poly-AU and Poly-UG, respectively. Consequently, in this case, THN-cysteine would substitute for isoleucine and valine during protein synthesis.
有证据表明，1,2-环氧-THN与半胱氨酸反应形成的S-(1,2,3,4-四氢-2-羟基-1-萘基)-L-半胱氨酸（THN-半胱氨酸）可掺入蛋白质中；THN-半胱氨酸掺入蛋白质的位置取决于THN的环氧化物是与半胱氨酰-tRNACyS反应还是与半胱氨酸反应。在这两种情况下，THN-半胱氨酸掺入蛋白质的机制与天然氨基酸相同。例如，Poly-UG（tRNACyS的密码子）可刺激THN-半胱氨酰-tRNACyS的掺入，预计它会在正在合成的蛋白质中替代半胱氨酸，而先前未酯化到tRNA的THN-半胱氨酸则由异亮氨酰和缬氨酰-RNA合成酶激活，其掺入分别受Poly-AU和Poly-UG刺激。因此，在这种情况下，THN-半胱氨酸在蛋白质合成过程中会替代异亮氨酸和缬氨酸。
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