Olson H M, Grant P G, Glitz D G, Cooperman B S
Proc Natl Acad Sci U S A. 1980 Feb;77(2):890-4. doi: 10.1073/pnas.77.2.890.
Ribosomes from Escherichia coli strain TPR201 (which lack N6,N6-dimethyladenosine) have been photoaffinity labeled with [3H]puromycin in the presence of chloramphenicol. Puromycin-modified 30S ribosomal subunits appear to be identical to untreated subunits in electron micrographs and are efficiently precipitated by antibodies to the puromycin analog N6,N6-dimethyladenosine. Electron micrographs of subunit-antibody complexes show ribosomal subunits to which an individual antibody molecule is bound and pairs of 30S subunits which appear to be crosslinked by a single IgG molecule. A predominant site of puromycin photoaffinity labeling has been identified from the apparent point of contact of antibody and ribosomal subunit. The puromycin site is localized to the small upper portion of the particle on the side opposite to the subunit platform. This location is close to that reported for ribosomal protein S14, the major puromycin-labeled protein in the small ribosomal subunit.
来自大肠杆菌TPR20菌株（缺乏N6,N6 - 二甲基腺苷）的核糖体已在氯霉素存在的情况下用[3H]嘌呤霉素进行光亲和标记。在电子显微镜下，嘌呤霉素修饰的30S核糖体亚基似乎与未处理的亚基相同，并且能被针对嘌呤霉素类似物N6,N6 - 二甲基腺苷的抗体有效沉淀。亚基 - 抗体复合物的电子显微镜照片显示，单个抗体分子结合到核糖体亚基上，并且成对的30S亚基似乎由单个IgG分子交联。已从抗体与核糖体亚基的明显接触点确定了嘌呤霉素光亲和标记的主要位点。嘌呤霉素位点位于颗粒与亚基平台相对一侧的小上部。该位置与核糖体蛋白S14的报道位置相近，核糖体蛋白S14是小核糖体亚基中主要的嘌呤霉素标记蛋白。
