@techreport{oai:soar-ir.repo.nii.ac.jp:00014591,
 author = {野村,  隆臣 and 清水,  知視 and 八森,  章},
 month = {Mar},
 note = {Silkworm (Bombyx mori) has an efficient protein synthesis 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 synthesis in the cell, two unique base exchanges were detected in the GTPase domain, which is one of the the functional ribosomal RNA domains highly conserved in all organisms. This domain is related with translational factors dependent GTP hydrolysis linked translational speed. Therefore, it is thought that an efficient protein synthesis ability of silkworm strongly arises from detected base exchange. Moreover, we also investigated the assembly mechanism of this domain binding proteins, P proteins (P0, P1, P2). Resultly, it was revealed that two P1-P2 hetero-dimers bound to two different regions of P0, one binding site existed in 55-65 amino acids and another site in 81-107 amino acids from C-terminus of P0., Article, 先進ファイバー工学研究教育拠点研究成果報告書 10: 65-65(2004)},
 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 = {2004}
}