IDENTIFICATION OF A SOLUBLE-PROTEIN THAT STIMULATES PEPTIDE-BOND SYNTHESIS
IDENTIFICATION OF A SOLUBLE-PROTEIN THAT STIMULATES PEPTIDE-BOND SYNTHESIS
复制标题
DOI：
10.1073/pnas.72.11.4257
复制
发表时间：
1975-01-01
影响因子：
11.1
通讯作者：
GANOZA, MC
中科院分区：
文献类型：
--
作者：
GLICK, BR;GANOZA, MC
分离出一种不含延伸因子（EF）-T和EF-G的可溶性蛋白因子，该蛋白因子能够使用核糖体结合的70 S-AUG-N-甲酰基-[35 S]甲硫氨酰-tRNA复合物和添加的嘌呤霉素作为底物刺激肽键合成。在大肠杆菌提取物的无核糖体细胞质中发现超过90%的这种活性。分子量、纯化特性和催化活性等特征将该因子与核糖体蛋白和已知的翻译激活剂区分开来。该因子需要肽键合成所需的所有组分，并且被已知特异性阻断核糖体的肽基转移酶活性的抗生素抑制。该因子使核糖体对氨酰-tRNA类似物嘌呤霉素的结合亲和力增加约10倍。我们认为，这种胞外因子调节核糖体的内在活性，催化肽键的合成，并把它作为一个新的因素所需的肽链延长，我们称之为EF-P。
A soluble protein factor was isolated, free of elongation factor (EF)-T and EF-G, based on its ability to stimulate the synthesis of peptide bonds using ribosomal bound 70S-AUG-N-formyl-[35S]methionyl-tRNA complex and added puromycin as substrates. Over 90% of this activity was found in the ribosome-free cytoplasm of Escherichia coli extracts. Otherfeatures such as molecular weight, purification properties, and catalytic activities distinguish this factor from ribosomal proteins and known activators of translation. The factor requires all components needed for peptide bond synthesis and is inhibited by antibiotics known to specifically block the peptidyl transferase activity of ribosomes. The factor increases the binding affinity of the ribosome for the aminoacyl-tRNA analog puromycin about 10-fold. We suggest that this extraribosomal factor modulates the intrinsic activity of ribosomes to catalyze peptide-bond synthesis, and regard it as a new factor required for peptide chain elongation, which we call EF-P.