Anticodon-like binding of the HIV-1 tRNA-like element to human lysyl-tRNA synthetase

Liu, Sheng; Comandur, Roopa; Jones, Christopher P.; Tsang, Pearl; Musier‐Forsyth, Karin

doi:10.1261/rna.058081.116

Cited by 18 publications

(28 citation statements)

References 19 publications

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“…In particular, the tRNA Lys incorporation was dependent on the ability of KRS to bind to tRNA Lys , rather than its ability to aminoacylate tRNA Lys96 . Furthermore, KRS bound to a tRNA-like element located near the primer-binding site within the HIV-1 genomic RNA, thereby facilitating efficient annealing of tRNA Lys,3 to viral RNA prior to reverse transcription [97][98][99] (Fig. 3a).…”

Section: Arss and Infectious Diseases Arss In Virus Infectionmentioning

confidence: 99%

Roles of aminoacyl-tRNA synthetases in immune regulation and immune diseases

Nie

Sun

et al. 2019

Cell Death Dis

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Aminoacyl-tRNA synthetases (ARSs) play a vital role in protein synthesis by linking amino acids to their cognate transfer RNAs (tRNAs). This typical function has been well recognized over the past few decades. However, accumulating evidence reveals that ARSs are involved in a wide range of physiological and pathological processes apart from translation. Strikingly, certain ARSs are closely related to different types of immune responses. In this review, we address the infection and immune responses induced by pathogen ARSs, as well as the potential anti-infective compounds that target pathogen ARSs. Meanwhile, we describe the functional mechanisms of ARSs in the development of immune cells. In addition, we focus on the roles of ARSs in certain immune diseases, such as autoimmune diseases, infectious diseases, and tumor immunity. Although our knowledge of ARSs in the immunological context is still in its infancy, research in this field may provide new ideas for the treatment of immune-related diseases.

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Section: Arss and Infectious Diseases Arss In Virus Infectionmentioning

confidence: 99%

Roles of aminoacyl-tRNA synthetases in immune regulation and immune diseases

Nie

Sun

et al. 2019

Cell Death Dis

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“…Two tRNA-like structures in the mRNA leader sequence of the ThrS enzyme compete with tRNA Thr for ThrS ( Springer et al, 1989 , 1998 ). An example of the other part, that of intersection between the biology of viral RNAs and tRNA is found HIV ( Liu et al, 2016 ). The retrotranscription of the HIV-1 virus RNA needs tRNA Lys as a primer for the reverse transcriptase enzyme.…”

Section: Hypothetical Communicative Mechanism Involving Trna-like-mrnmentioning

confidence: 99%

“…The virion contains copies of this tRNA to initiate the reproductive cycle in the newly infected cell, but this tRNA travels as a complex with the Lysyl-tRNA synthetase. So that this tRNA Lys can be released from the complex, it needs the help of a tRNA-like element in the 5’ UTR region of the HIV mRNA, which competes with the interaction of that complex ( Liu et al, 2016 ).…”

Section: Hypothetical Communicative Mechanism Involving Trna-like-mrnmentioning

confidence: 99%

Viral tRNA Mimicry from a Biocommunicative Perspective

Ariza-Mateos

Gómez

2017

Front. Microbiol.

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RNA viruses have very small genomes which limits the functions they can encode. One of the strategies employed by these viruses is to mimic key factors of the host cell so they can take advantage of the interactions and activities these factors typically participate in. The viral RNA genome itself was first observed to mimic cellular tRNA over 40 years ago. Since then researchers have confirmed that distinct families of RNA viruses are accessible to a battery of cellular factors involved in tRNA-related activities. Recently, potential tRNA-like structures have been detected within the sequences of a 100 mRNAs taken from human cells, one of these being the host defense interferon-alpha mRNA; these are then additional to the examples found in bacterial and yeast mRNAs. The mimetic relationship between tRNA, cellular mRNA, and viral RNA is the central focus of two considerations described below. These are subsequently used as a preface for a final hypothesis drawing on concepts relating to mimicry from the social sciences and humanities, such as power relations and creativity. Firstly, the presence of tRNA-like structures in mRNAs indicates that the viral tRNA-like signal could be mimicking tRNA-like elements that are contextualized by the specific carrier mRNAs, rather than, or in addition to, the tRNA itself, which would significantly increase the number of potential semiotic relations mediated by the viral signals. Secondly, and in particular, mimicking a host defense mRNA could be considered a potential new viral strategy for survival. Finally, we propose that mRNA’s mimicry of tRNA could be indicative of an ancestral intracellular conflict in which species of mRNAs invaded the cell, but from within. As the meaning of the mimetic signal depends on the context, in this case, the conflict that arises when the viral signal enters the cell can change the meaning of the mRNAs’ internal tRNA-like signals, from their current significance to that they had in the distant past.

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“…could be selectively packed into the HIV-1 virion. LysRS, tRNA Lys3 , viral precursor proteins Gag, and GagPol form a cytoplasmic nucleoprotein complex to facilitate the HIV viral reverse transcription after infecting new host cells (21)(22)(23). In mast cells, IgE-antigen stimulation activates specific phosphorylation of LysRS on a Ser 207 residue (24).…”

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confidence: 99%

Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex

Hei

Liu

et al. 2019

Journal of Biological Chemistry

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Edited by Karin Musier-Forsyth Multi-aminoacyl-tRNA synthetase complex (MSC) is the second largest machinery for protein synthesis in human cells and also regulates multiple nontranslational functions through its components. Previous studies have shown that the MSC can respond to external signals by releasing its components to function outside it. The internal assembly is fundamental to MSC regulation. Here, using crystal structural analyses (at 1.88 Å resolution) along with molecular modeling, gel-filtration chromatography, and co-immunoprecipitation, we report that human lysyl-tRNA synthetase (LysRS) forms a tighter assembly with the scaffold protein aminoacyl-tRNA synthetase complex-interacting multifunctional protein 2 (AIMP2) than previously observed. We found that two AIMP2 N-terminal peptides form an antiparallel scaffold and hold two LysRS dimers through four binding motifs and additional interactions. Of note, the four catalytic subunits of LysRS in the tightly assembled complex were all accessible for tRNA recognition. We further noted that two recently reported human disease-associated mutations conflict with this tighter assembly, cause LysRS release from the MSC, and inactivate the enzyme. These findings reveal a previously unknown dimension of MSC subcomplex assembly and suggest that the retractility of this complex may be critical for its physiological functions. cro ARTICLE

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Anticodon-like binding of the HIV-1 tRNA-like element to human lysyl-tRNA synthetase

Cited by 18 publications

References 19 publications

Roles of aminoacyl-tRNA synthetases in immune regulation and immune diseases

Roles of aminoacyl-tRNA synthetases in immune regulation and immune diseases

Viral tRNA Mimicry from a Biocommunicative Perspective

Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex

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