@techreport{oai:soar-ir.repo.nii.ac.jp:00014478,
 author = {野村,  隆臣 and 清水,  知視 and 八森,  章},
 month = {Mar},
 note = {Silkworm (Bombyx mori) has an efficient translation system because silkworm can synthesize numerous silk proteins (fibroin) in a short period of time. By analyses of its Ribosome  that plays a central role of protein biosynthesis in the cell, two unique base exchanges (U1094C and A1098G) were detected in the GTPase domain (1070 region ; E. coli numbering), which is universal conserved ribosomal RNA (rRNA) domain related with translational factors dependent GTP hydrolysis linked translational speed. We constructed E. Coli ribosome introduced their base exchanges to GTPase domain, and analysed its ribosomal function. Resultly, E. coli ribosome harvested C1094/G1098 showed, compared with wild type, 30-40 % of activities in dependent on elongation factors and 15 % in translation of natural mRNA. By these result, it was suggested that C1097/G1098 base exchange was relative to a regulation rather than an efficiency of the protein biosynthesis., Article, 先進ファイバー工学研究教育拠点研究成果報告書 11: 63-63(2005)},
 title = {15-2-17 : 蚕タンパク質合成系の生化学的解析とその応用},
 year = {2005}
}