Differential Modes of Transfer RNASer Recognition in Methanosarcina barkeri
TLDR
It is proposed that such a distinction between the two enzymes in tRNASer identity determinants reflects their evolutionary pathways, hence attesting to their diversity.About:
This article is published in Journal of Biological Chemistry.The article was published on 2004-11-19 and is currently open access. It has received 33 citations till now. The article focuses on the topics: Methanosarcina barkeri.read more
Citations
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Natural expansion of the genetic code.
TL;DR: The existence of phosphoseryl-tRNA (in the form of tRNACys and tRNASec) may presage the discovery of other cotranslationally inserted modified amino acids.
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Biased gene transfer in microbial evolution.
TL;DR: There is evidence that prokaryotes (bacteria and archaea) are more likely to transfer genetic material with their close relatives than with distantly related lineages, which can create phylogenetic signals that are difficult to distinguish from the signal created through shared ancestry.
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Dual-mode recognition of noncanonical tRNAsSer by seryl-tRNA synthetase in mammalian mitochondria
Sarin Chimnaronk,Mads Gravers Jeppesen,Tsutomu Suzuki,Jens Nyborg,Kimitsuna Watanabe,Kimitsuna Watanabe +5 more
TL;DR: The key elements that establish tRNA binding specificity, differ from all other known bacterial and eukaryotic systems, are the characteristic extensions in both extremities, as well as a few basic residues residing in the amino‐terminal helical arm of mt SerRS.
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Structure of the Unusual Seryl-tRNA Synthetase Reveals a Distinct Zinc-Dependent Mode of Substrate Recognition
Silvija Bilokapic,Timm Maier,Dragana Ahel,Dragana Ahel,Ita Gruić-Sovulj,Dieter Söll,Ivana Weygand-Durasevic,Nenad Ban +7 more
TL;DR: SerRS represents the only known aminoacyl‐tRNA synthetase system that evolved two distinct mechanisms for the recognition of the same amino‐acid substrate.
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Emergence of the universal genetic code imprinted in an RNA record
TL;DR: In this article, the identity elements of Methanocaldococcus jannaschii tRNACys were determined in the aminoacylation reaction for the two Methanococcus maripaludis synthetases SepRS (forming Sep-tRNAACys) and Cys-tRNACYS.
References
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Universal rules and idiosyncratic features in tRNA identity
TL;DR: This survey describes the molecular signals in tRNAs that trigger specific aminoacylations, and shows that alternate identity sets can be recognized by a single synthetase, and emphasize the importance of tRNA architecture and anti-determinants preventing false recognition.
Book
Trna: Structure, Biosynthesis, and Function
Dieter Söll,Uttam L. RajBhandary +1 more
TL;DR: The tRNA identity problem: past, present and future Small RNA oligonucleotide substrates for specific aminoacylations tRNA discrimination in aminoacylation Recognition in the glutamine tRNA system: from structure to function
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Aminoacyl-tRNA Synthetases, the Genetic Code, and the Evolutionary Process
TL;DR: These findings are used to refine the theory that at the evolutionary stage represented by the root of the universal phylogenetic tree, cells were far more primitive than their modern counterparts and thus exchanged genetic material in far less restricted ways, in effect evolving in a communal sense.
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The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser).
TL;DR: The structure revealed how insertion of conserved base G20b from the D loop into the core of the tRNA determines the orientation of the long variable arm, which is a characteristic feature of most serine specific tRNAs.
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Changing the identity of a transfer RNA
TL;DR: A leucine transferRNA has been transformed into a serine transfer RNA by changing 12 nucleotides, indicating that a limited set of residues determine tRNA identity.