|Title:||Functional importance of mobile ribosomal proteins||Authors:||Chang, K.-C.
|Issue Date:||2015||Journal Volume:||2015||Source:||BioMed Research International||Abstract:||
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. © 2015 Kai-Chun Chang et al.
|ISSN:||23146133||DOI:||10.1155/2015/539238||SDG/Keyword:||bacterial protein; guanosine triphosphatase; ribosomal protein L1; ribosomal protein L12; ribosomal protein L9; ribosomal protein S1; ribosome protein; transfer RNA; unclassified drug; protein binding; ribosome protein; ribosome RNA; allosterism; carboxy terminal sequence; dissociation; nonhuman; protein function; Review; ribosome; RNA transport; translation regulation; animal; binding site; biological model; catalysis; chemical model; chemistry; computer simulation; human; metabolism; molecular model; physiology; protein conformation; structure activity relation; ultrastructure; Allosteric Regulation; Animals; Binding Sites; Catalysis; Computer Simulation; Humans; Models, Biological; Models, Chemical; Models, Molecular; Protein Binding; Protein Conformation; Ribosomal Proteins; Ribosomes; RNA, Ribosomal; Structure-Activity Relationship|
|Appears in Collections:||分子與細胞生物學研究所|
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