Mechanistic Insights Into Catalytic RNA-Protein Complexes Involved in Translation of the Genetic Code
- PMID: 28683922
- DOI: 10.1016/bs.apcsb.2017.04.002
Mechanistic Insights Into Catalytic RNA-Protein Complexes Involved in Translation of the Genetic Code
Abstract
The contemporary world is an "RNA-protein world" rather than a "protein world" and tracing its evolutionary origins is of great interest and importance. The different RNAs that function in close collaboration with proteins are involved in several key physiological processes, including catalysis. Ribosome-the complex megadalton cellular machinery that translates genetic information encoded in nucleotide sequence to amino acid sequence-epitomizes such an association between RNA and protein. RNAs that can catalyze biochemical reactions are known as ribozymes. They usually employ general acid-base catalytic mechanism, often involving the 2'-OH of RNA that activates and/or stabilizes a nucleophile during the reaction pathway. The protein component of such RNA-protein complexes (RNPCs) mostly serves as a scaffold which provides an environment conducive for the RNA to function, or as a mediator for other interacting partners. In this review, we describe those RNPCs that are involved at different stages of protein biosynthesis and in which RNA performs the catalytic function; the focus of the account is on highlighting mechanistic aspects of these complexes. We also provide a perspective on such associations in the context of proofreading during translation of the genetic code. The latter aspect is not much appreciated and recent works suggest that this is an avenue worth exploring, since an understanding of the subject can provide useful insights into how RNAs collaborate with proteins to ensure fidelity during these essential cellular processes. It may also aid in comprehending evolutionary aspects of such associations.
Keywords: Catalysis; DTD; Editing/proofreading; Genetic code; RNA; RNase P; Ribosome; Spliceosome; Synthetase; Translation.
© 2017 Elsevier Inc. All rights reserved.
Similar articles
-
Enzyme action at RNA-protein interface in DTD-like fold.Curr Opin Struct Biol. 2018 Dec;53:107-114. doi: 10.1016/j.sbi.2018.07.013. Epub 2018 Aug 16. Curr Opin Struct Biol. 2018. PMID: 30121401 Review.
-
Structural Roles of Noncoding RNAs in the Heart of Enzymatic Complexes.Biochemistry. 2017 Jan 10;56(1):3-13. doi: 10.1021/acs.biochem.6b01106. Epub 2016 Dec 29. Biochemistry. 2017. PMID: 27935277 Free PMC article.
-
Mechanistic insights into precursor messenger RNA splicing by the spliceosome.Nat Rev Mol Cell Biol. 2017 Nov;18(11):655-670. doi: 10.1038/nrm.2017.86. Epub 2017 Sep 27. Nat Rev Mol Cell Biol. 2017. PMID: 28951565 Review.
-
Mechanisms of catalytic RNA molecules.Biochem Soc Trans. 2021 Aug 27;49(4):1529-1535. doi: 10.1042/BST20200465. Biochem Soc Trans. 2021. PMID: 34415304 Free PMC article. Review.
-
The catalytic diversity of RNAs.Nat Rev Mol Cell Biol. 2005 May;6(5):399-412. doi: 10.1038/nrm1647. Nat Rev Mol Cell Biol. 2005. PMID: 15956979 Review.
Cited by
-
Chiral checkpoints during protein biosynthesis.J Biol Chem. 2019 Nov 8;294(45):16535-16548. doi: 10.1074/jbc.REV119.008166. Epub 2019 Oct 7. J Biol Chem. 2019. PMID: 31591268 Free PMC article. Review.
-
A discriminator code-based DTD surveillance ensures faithful glycine delivery for protein biosynthesis in bacteria.Elife. 2018 Aug 9;7:e38232. doi: 10.7554/eLife.38232. Elife. 2018. PMID: 30091703 Free PMC article.
-
The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches.Front Mol Biosci. 2021 Apr 7;8:661448. doi: 10.3389/fmolb.2021.661448. eCollection 2021. Front Mol Biosci. 2021. PMID: 33898526 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
