Structural basis of Sec-independent membrane protein insertion by YidC

[プレスリリース]バイオサイエンス研究科膜分子複合機能学研究室の塚崎智也准教授らの研究グループが、タンパク質を細胞膜に組み込むメカニズムを解明しました（2014/04/17）Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates into the membrane, thereby facilitating membrane protein assembly in bacteria; the homologous proteins Oxa1 and Alb3 have the same function in mitochondria and chloroplasts, respectively1, 2. In the bacterial cytoplasmic membrane, YidC functions as an independent insertase and a membrane chaperone in cooperation with the translocon SecYEG3, 4, 5. Here we present the crystal structure of YidC from Bacillus halodurans, at 2.4 Å resolution. The structure reveals a novel fold, in which five conserved transmembrane helices form a positively charged hydrophilic groove that is open towards both the lipid bilayer and the cytoplasm but closed on the extracellular side. Structure-based in vivo analyses reveal that a conserved arginine residue in the groove is important for the insertion of membrane proteins by YidC. We propose an insertion mechanism for single-spanning membrane proteins, in which the hydrophilic environment generated by the groove recruits the extracellular regions of substrates into the low-dielectric environment of the membrane

電気的作成血栓による脳動脈瘤ならびに脳動静脈奇形の治療に関する実験的研究

京都大学0048新制・課程博士医学博士甲第679号医博第296号新制||医||118(附属図書館)1369UT51-51-L113京都大学大学院医学研究科外科系専攻(主査)教授 半田 肇, 教授 木村 忠司, 教授 本庄 一夫学位規則第5条第1項該当Kyoto UniversityDA

電気的作成血栓による脳動脈瘤ならびに脳動静脈奇形の治療に関する実験的研究

京都大学0048新制・課程博士医学博士甲第679号医博第296号新制||医||118(附属図書館)1369UT51-51-L113京都大学大学院医学研究科外科系専攻(主査)教授 半田 肇, 教授 木村 忠司, 教授 本庄 一夫学位規則第5条第1項該当Kyoto UniversityDA