Van Noort J M, Kraal B, Bosch L, La Cour T F, Nyborg J, Clark B F
Proc Natl Acad Sci U S A. 1984 Jul;81(13):3969-72. doi: 10.1073/pnas.81.13.3969.
Recently, we reported on the induction by kirromycin of two tRNA binding sites on elongation factor Tu. To obtain independent information on the existence of these two sites and to characterize them further, 3' oxidized tRNA was cross-linked to elongation factor Tu by [3H]borohydride reduction. Specific cross-linking occurred exclusively in the presence of kirromycin. In the case of elongation factor Tu X GDP X kirromycin, cross-linking was found at lysine-208; in elongation factor Tu X GTP X kirromycin, cross-linking was at lysine-208 and lysine-237. In both elongation factor Tu complexes, kirromycin itself was found cross-linked to lysine-357. The tRNA cross-linking sites are in agreement with the idea of two different binding sites of tRNA on elongation factor Tu.
最近,我们报道了奇霉素诱导延伸因子Tu上两个tRNA结合位点的情况。为了获得关于这两个位点存在的独立信息并进一步对其进行表征,通过[³H]硼氢化还原将3'氧化的tRNA与延伸因子Tu交联。特异性交联仅在奇霉素存在时发生。在延伸因子Tu·GDP·奇霉素的情况下,交联发生在赖氨酸-208处;在延伸因子Tu·GTP·奇霉素中,交联发生在赖氨酸-208和赖氨酸-237处。在这两种延伸因子Tu复合物中,均发现奇霉素自身与赖氨酸-357交联。tRNA交联位点与tRNA在延伸因子Tu上存在两个不同结合位点的观点一致。