Functional Importance of Mobile Ribosomal Proteins.
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 str...
| Publicado en: | BioMed Research International Vol. 2015; pp. 1 - 12 |
|---|---|
| Autores principales: | , , |
| Formato: | equations & formulas pictorial review Journal Article |
| Publicado: |
Wiley-Blackwell
9/20/2015
|
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=110155484&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 110155484 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 9/20/2015 vid: 2015 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 110155484 110155484 NLM26457300 110155484 10.1155/2015/539238 NLM26457300 PMC4592705 110155484 ppf: 1 ppct: 11 formats: fmt: @attributes: type: P tig: atl: Functional Importance of Mobile Ribosomal Proteins. aug: au: Chang, Kai-Chun Wen, Jin-Der Yang, Lee-Wei affil: Institute of Molecular and Cellular Biology, National Taiwan University, Taipei 10617, Taiwan sug: subj: Proteins Physiology Cytoplasm Physiology Proteins Metabolism Cytoplasm Metabolism RNA Physiology Biochemical Phenomena ab: 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. pubtype: Academic Journal doctype: equations & formulas pictorial review Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
|---|