The DOI matches its Crossref record; 283 of the 283 references it cites were found in a registry or an index.
Transfer RNA Modification
Abstract
Transfer RNA (tRNA) from all organisms on this planet contains modified nucleosides, which are derivatives of the four major nucleosides. tRNA from Escherichia coli/Salmonella enterica contains 31 different modified nucleosides, which are all, except for one (Queuosine[Q]), synthesized on an oligonucleotide precursor, which through specific enzymes later matures into tRNA. The corresponding structural genes for these enzymes are found in mono- and polycistronic operons, the latter of which have a complex transcription and translation pattern. The syntheses of some of them (e.g.,several methylated derivatives) are catalyzed by one enzyme, which is position and base specific, but synthesis of some have a very complex biosynthetic pathway involving several enzymes (e.g., 2-thiouridines, N 6 -threonyladenosine [t6A],and Q). Several of the modified nucleosides are essential for viability (e.g.,lysidin, t 6 A, 1-methylguanosine), whereas deficiency in others induces severe growth defects. However, some have no or only a small effect on growth at laboratory conditions. Modified nucleosides that are present in the anticodon loop or stem have a fundamental influence on the efficiency of charging the tRNA, reading cognate codons, and preventing missense and frameshift errors. Those, which are present in the body of the tRNA, have a primarily stabilizing effect on the tRNA. Thus, the ubiquitouspresence of these modified nucleosides plays a pivotal role in the function of the tRNA by their influence on the stability and activity of the tRNA.
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Metadata
- Authors
- Björk, G. R., & Hagervall, T. G.
- Venue
- EcoSal Plus
- Publisher
- American Society for Microbiology
- Published
- 2005-01-12
- Volume
- 1
- Issue
- 2
- Pages
- 263-87
- ISSN
- 2324-6200 (ISSN-L)
- OpenAlex
- W1971559304
- Cited by
- 340
- References
- 283
- FWCI
- 4.38
- Type
- journal article
- Language
- en
- Open access
- closed
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