Ribosome evolution: Emergence of peptide synthesis machinery
Journal of Biosciences, ISSN: 0250-5991, Vol: 36, Issue: 5, Page: 921-928
2011
- 38Citations
- 68Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations38
- Citation Indexes38
- 38
- CrossRef32
- Captures68
- Readers68
- 68
Review Description
Proteins, the main players in current biological systems, are produced on ribosomes by sequential amide bond (peptide bond) formations between amino-acid-bearing tRNAs. The ribosome is an exquisite super-complex of RNA-proteins, containing more than 50 proteins and at least 3 kinds of RNAs. The combination of a variety of side chains of amino acids (typically 20 kinds with some exceptions) confers proteins with extraordinary structure and functions. The origin of peptide bond formation and the ribosome is crucial to the understanding of life itself. In this article, a possible evolutionary pathway to peptide bond formation machinery (proto-ribosome) will be discussed, with a special focus on the RNA minihelix (primordial form of modern tRNA) as a starting molecule. Combining the present data with recent experimental data, we can infer that the peptidyl transferase center (PTC) evolved from a primitive system in the RNA world comprising tRNA-like molecules formed by duplication of minihelix-like small RNA. © Indian Academy of Sciences.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84858730787&origin=inward; http://dx.doi.org/10.1007/s12038-011-9158-2; http://www.ncbi.nlm.nih.gov/pubmed/22116290; http://link.springer.com/10.1007/s12038-011-9158-2; https://dx.doi.org/10.1007/s12038-011-9158-2; https://link.springer.com/article/10.1007/s12038-011-9158-2; http://www.springerlink.com/index/10.1007/s12038-011-9158-2; http://www.springerlink.com/index/pdf/10.1007/s12038-011-9158-2
Springer Science and Business Media LLC
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