E-Mail Alert

Add your e-mail address to receive forthcoming issues of this journal:

Journal Browser

Journal Browser

Special Issue "Functions of Transfer RNAs 2.0"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (31 March 2018).

Special Issue Editor

Guest Editor
Prof. Dr. Lluís Ribas de Pouplana

Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Parc Científic de Barcelona, C/Baldiri Reixac 10, 08028 Barcelona, Catalonia, Spain
Website | E-Mail
Interests: genetic code; genetic translation; codon usage; proteome control; tRNAs; ribosomes; proteome quality control in cell biology and disease; structure-function studies of protein-RNA interactions; biomedicine and biotechnology

Special Issue Information

Dear Colleagues,

Transfer RNA (tRNA) has been in the focus of molecular biology since its central role in translating the genetic code was first predicted by Crick, over 60 years ago. Despite this long history, exciting new revelations continue to be discovered around tRNA, a consequence of its intricate integration with all aspects of cell biology.

Current interest in tRNA is far from limited to its canonical role in translation, and extends now to metabolism, cell signaling, stress responses, and a range of medical conditions from infectious diseases to cancer. Continuing from an issue of IJMS that was published to celebrate the 50th anniversary of the international tRNA meeting, we will assemble a second collection of articles to summarize the state-of-the-art regarding the many angles that tRNA research takes today. Once again, this issue will cover the evolution of the molecule and the genetic code, tRNA synthesis and cellular distribution, roles in translation, signaling connections between tRNAs and regulatory pathways, roles in disease, and biotechnological advances. We hope to provide, once again, a useful compilation of the latest developments in tRNA biology.

Prof. Dr. Lluís Ribas de Pouplana
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • transfer RNA
  • structure-function
  • genes
  • maturation
  • mutation
  • translation
  • genetic code
  • codon recognition
  • aminoacyl-tRNA synthesis
  • protein synthesis
  • biosynthesis
  • synthetic biology
  • tRNA-dependent regulation
  • posttranscriptional modifications

Published Papers (3 papers)

View options order results:
result details:
Displaying articles 1-3
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle
A Temporal Order in 5′- and 3′- Processing of Eukaryotic tRNAHis
Int. J. Mol. Sci. 2019, 20(6), 1384; https://doi.org/10.3390/ijms20061384
Received: 26 January 2019 / Revised: 21 February 2019 / Accepted: 15 March 2019 / Published: 19 March 2019
PDF Full-text (1331 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
For flawless translation of mRNA sequence into protein, tRNAs must undergo a series of essential maturation steps to be properly recognized and aminoacylated by aminoacyl-tRNA synthetase, and subsequently utilized by the ribosome. While all tRNAs carry a 3′-terminal CCA sequence that includes the [...] Read more.
For flawless translation of mRNA sequence into protein, tRNAs must undergo a series of essential maturation steps to be properly recognized and aminoacylated by aminoacyl-tRNA synthetase, and subsequently utilized by the ribosome. While all tRNAs carry a 3′-terminal CCA sequence that includes the site of aminoacylation, the additional 5′-G-1 position is a unique feature of most histidine tRNA species, serving as an identity element for the corresponding synthetase. In eukaryotes including yeast, both 3′-CCA and 5′-G-1 are added post-transcriptionally by tRNA nucleotidyltransferase and tRNAHis guanylyltransferase, respectively. Hence, it is possible that these two cytosolic enzymes compete for the same tRNA. Here, we investigate substrate preferences associated with CCA and G-1-addition to yeast cytosolic tRNAHis, which might result in a temporal order to these important processing events. We show that tRNA nucleotidyltransferase accepts tRNAHis transcripts independent of the presence of G-1; however, tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. Although many tRNA maturation steps can occur in a rather random order, our data demonstrate a likely pathway where CCA-addition precedes G-1 incorporation in S. cerevisiae. Evidently, the 3′-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. Full article
(This article belongs to the Special Issue Functions of Transfer RNAs 2.0)
Figures

Graphical abstract

Review

Jump to: Research

Open AccessReview
7-Methylguanosine Modifications in Transfer RNA (tRNA)
Int. J. Mol. Sci. 2018, 19(12), 4080; https://doi.org/10.3390/ijms19124080
Received: 13 November 2018 / Revised: 5 December 2018 / Accepted: 13 December 2018 / Published: 17 December 2018
Cited by 2 | PDF Full-text (1827 KB) | HTML Full-text | XML Full-text
Abstract
More than 90 different modified nucleosides have been identified in tRNA. Among the tRNA modifications, the 7-methylguanosine (m7G) modification is found widely in eubacteria, eukaryotes, and a few archaea. In most cases, the m7G modification occurs at position 46 [...] Read more.
More than 90 different modified nucleosides have been identified in tRNA. Among the tRNA modifications, the 7-methylguanosine (m7G) modification is found widely in eubacteria, eukaryotes, and a few archaea. In most cases, the m7G modification occurs at position 46 in the variable region and is a product of tRNA (m7G46) methyltransferase. The m7G46 modification forms a tertiary base pair with C13-G22, and stabilizes the tRNA structure. A reaction mechanism for eubacterial tRNA m7G methyltransferase has been proposed based on the results of biochemical, bioinformatic, and structural studies. However, an experimentally determined mechanism of methyl-transfer remains to be ascertained. The physiological functions of m7G46 in tRNA have started to be determined over the past decade. For example, tRNA m7G46 or tRNA (m7G46) methyltransferase controls the amount of other tRNA modifications in thermophilic bacteria, contributes to the pathogenic infectivity, and is also associated with several diseases. In this review, information of tRNA m7G modifications and tRNA m7G methyltransferases is summarized and the differences in reaction mechanism between tRNA m7G methyltransferase and rRNA or mRNA m7G methylation enzyme are discussed. Full article
(This article belongs to the Special Issue Functions of Transfer RNAs 2.0)
Figures

Figure 1

Open AccessReview
Impact of tRNA Modifications and tRNA-Modifying Enzymes on Proteostasis and Human Disease
Int. J. Mol. Sci. 2018, 19(12), 3738; https://doi.org/10.3390/ijms19123738
Received: 31 October 2018 / Revised: 17 November 2018 / Accepted: 20 November 2018 / Published: 24 November 2018
Cited by 5 | PDF Full-text (1707 KB) | HTML Full-text | XML Full-text
Abstract
Transfer RNAs (tRNAs) are key players of protein synthesis, as they decode the genetic information organized in mRNA codons, translating them into the code of 20 amino acids. To be fully active, tRNAs undergo extensive post-transcriptional modifications, catalyzed by different tRNA-modifying enzymes. Lack [...] Read more.
Transfer RNAs (tRNAs) are key players of protein synthesis, as they decode the genetic information organized in mRNA codons, translating them into the code of 20 amino acids. To be fully active, tRNAs undergo extensive post-transcriptional modifications, catalyzed by different tRNA-modifying enzymes. Lack of these modifications increases the level of missense errors and affects codon decoding rate, contributing to protein aggregation with deleterious consequences to the cell. Recent works show that tRNA hypomodification and tRNA-modifying-enzyme deregulation occur in several diseases where proteostasis is affected, namely, neurodegenerative and metabolic diseases. In this review, we discuss the recent findings that correlate aberrant tRNA modification with proteostasis imbalances, in particular in neurological and metabolic disorders, and highlight the association between tRNAs, their modifying enzymes, translational decoding, and disease onset. Full article
(This article belongs to the Special Issue Functions of Transfer RNAs 2.0)
Figures

Graphical abstract

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top