Functional Importance of Mobile Ribosomal Proteins

被引:9
作者
Chang, Kai-Chun [1 ]
Wen, Jin-Der [1 ]
Yang, Lee-Wei [2 ]
机构
[1] Natl Taiwan Univ, Inst Mol & Cellular Biol, Taipei 10617, Taiwan
[2] Natl Tsing Hua Univ, Inst Bioinformat & Struct Biol, Hsinchu 30013, Taiwan
关键词
NORMAL-MODE ANALYSIS; PEPTIDE-BOND FORMATION; TRANSFER-RNA DYNAMICS; MESSENGER-RNA; ESCHERICHIA-COLI; STRUCTURAL BASIS; L1; STALK; CRYSTAL-STRUCTURE; INTERMEDIATE STATES; BACTERIAL RIBOSOME;
D O I
10.1155/2015/539238
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Although the dynamic motions and peptidyl transferase activity seem to be embedded in the rRNAs, the ribosome contains more than 50 ribosomal proteins (r-proteins), whose functions remain largely elusive. Also, the precise forms of some of these r-proteins, as being part of the ribosome, are not structurally solved due to their high flexibility, which hinders the efforts in their functional elucidation. Owing to recent advances in cryo-electron microscopy, single-molecule techniques, and theoretical modeling, much has been learned about the dynamics of these r-proteins. Surprisingly, allosteric regulations have been found in between spatially separated components as distant as those in the opposite sides of the ribosome. Here, we focus on the functional roles and intricate regulations of the mobile L1 and L12 stalks and L9 and S1 proteins. Conformational flexibility also enables versatile functions for r-proteins beyond translation. The arrangement of r-proteins may be under evolutionary pressure that fine-tunes mass distributions for optimal structural dynamics and catalytic activity of the ribosome.
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页数:11
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