Interaction Network of Human Aminoacyl-tRNA Synthetases and Subunits of Elongation Factor 1 Complex

Lee, Jong Sang; Park, Sang Gyu; Park, Heonyong; Seol, Wongi; Lee, Sang‐Won; Kim, Sung Hoon

doi:10.1006/bbrc.2002.6398

Cited by 44 publications

(16 citation statements)

References 30 publications

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“…Glutathione- S-transferase and glucosyl/glucuronosyl transferase, which are involved in xenobiotics detoxification, were up-regulated by 1.96 and 1.56-fold, respectively, in the resistant TH-2000 B. tabaci relative to the susceptible TH-S strain. Other up-regulated peptides in the resistant B. tabaci included UDP glucuronosyl transferase (1.73-fold), implicated in the inactivation and excretion of both endogenous and exogenous compounds [34]; luciferin regenerating enzyme (1.71-fold), playing an important role in the recycling of oxyluciferin into luciferin [35]; eukaryotic initiation factor (1.23-fold), associated with protein translation initiation and elongation processes [36]; glycyl-tRNA synthetase (1.38-fold), involved in RNA modification, RNA transportation, and amino acid-tRNA synthesis [37]; and ADP/ATP translocase proteins (1.49-fold), a group of enzymes catalyzing the exchange of ADP and ATP across the mitochondrial inner membrane [38]. In addition, proteins related to energy regulation, protein transportation and binding were also differentially expressed between the resistant and susceptible B. tabaci (Table S4).…”

Section: Resultsmentioning

confidence: 99%

Transcriptomic and Proteomic Responses of Sweetpotato Whitefly, Bemisia tabaci, to Thiamethoxam

et al. 2013

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BackgroundThe sweetpotato whitefly, Bemisia tabaci (Hemiptera: Aleyrodidae), is one of the most widely distributed agricultural pests. Although it has developed resistance to many registered insecticides including the neonicotinoid insecticide thiamethoxam, the mechanisms that regulate the resistance are poorly understood. To understand the molecular basis of thiamethoxam resistance, “omics” analyses were carried out to examine differences between resistant and susceptible B. tabaci at both transcriptional and translational levels.ResultsA total of 1,338 mRNAs and 52 proteins were differentially expressed between resistant and susceptible B. tabaci. Among them, 11 transcripts had concurrent transcription and translation profiles. KEGG analysis mapped 318 and 35 differentially expressed genes and proteins, respectively, to 160 and 59 pathways (p<0.05). Thiamethoxam treatment activated metabolic pathways (e.g., drug metabolism), in which 118 transcripts were putatively linked to insecticide resistance, including up-regulated glutathione-S-transferase, UDP glucuronosyltransferase, glucosyl/glucuronosyl transferase, and cytochrome P450. Gene Ontology analysis placed these genes and proteins into protein complex, metabolic process, cellular process, signaling, and response to stimulus categories. Quantitative real-time PCR analysis validated “omics” response, and suggested a highly overexpressed P450, CYP6CX1, as a candidate molecular basis for the mechanistic study of thiamethoxam resistance in whiteflies. Finally, enzymatic activity assays showed elevated detoxification activities in the resistant B. tabaci.ConclusionsThis study demonstrates the applicability of high-throughput omics tools for identifying molecular candidates related to thiamethoxam resistance in an agricultural important insect pest. In addition, transcriptomic and proteomic analyses provide a solid foundation for future functional investigations into the complex molecular mechanisms governing the neonicotinoid resistance in whiteflies.

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Section: Resultsmentioning

confidence: 99%

Transcriptomic and Proteomic Responses of Sweetpotato Whitefly, Bemisia tabaci, to Thiamethoxam

et al. 2013

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“…On the other hand, the standard proteins representing the stability of total phosphoproteins at 4°C were Pacsin1, Eefeld and Prpsap2. Eefeld delivers aminoacyl tRNAs to the ribosome [19], and is also known to catalyze the exchange of GDP bound to Elongation Factor 1α with GTP [20] which is stimulated by PKC [21]. Prpsap2 negatively regulates phosphoribosyl pyrophosphate (PRPP) synthetase [22].…”

Section: Resultsmentioning

confidence: 99%

Dynamic Changes of the Phosphoproteome in Postmortem Mouse Brains

et al. 2011

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Protein phosphorylation is deeply involved in the pathological mechanism of various neurodegenerative disorders. However, in human pathological samples, phosphorylation can be modified during preservation by postmortem factors such as time and temperature. Postmortem changes may also differ among proteins. Unfortunately, there is no comprehensive database that could support the analysis of protein phosphorylation in human brain samples from the standpoint of postmortem changes. As a first step toward addressing the issue, we performed phosphoproteome analysis with brain tissue dissected from mouse bodies preserved under different conditions. Quantitative whole proteome mass analysis showed surprisingly diverse postmortem changes in phosphoproteins that were dependent on temperature, time and protein species. Twelve hrs postmortem was a critical time point for preservation at room temperature. At 4°C, after the body was cooled down, most phosphoproteins were stable for 72 hrs. At either temperature, increase greater than 2-fold was exceptional during this interval. We found several standard proteins by which we can calculate the postmortem time at room temperature. The information obtained in this study will be indispensable for evaluating experimental data with human as well as mouse brain samples.

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“…1 ). Although some of those domains are thought to promote tRNA interactions [23,24] or to facilitate product transfer to the elongation factor [25–29], these domains in most cases are dispensable for aminoacylation. For those AARSs that are components of the MSC, the appended domains are involved in the formation of the complex [30,31].…”

Section: Functional Expansion Through Acquisition Of Extra Domainsmentioning

confidence: 99%

Functional expansion of human tRNA synthetases achieved by structural inventions

2009

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a b s t r a c tKnown as an essential component of the translational apparatus, the aminoacyl-tRNA synthetase family catalyzes the first step reaction in protein synthesis, that is, to specifically attach each amino acid to its cognate tRNA. While preserving this essential role, tRNA synthetases developed other roles during evolution. Human tRNA synthetases, in particular, have diverse functions in different pathways involving angiogenesis, inflammation and apoptosis. The functional diversity is further illustrated in the association with various diseases through genetic mutations that do not affect aminoacylation or protein synthesis. Here we review the accumulated knowledge on how human tRNA synthetases used structural inventions to achieve functional expansions.

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Interaction Network of Human Aminoacyl-tRNA Synthetases and Subunits of Elongation Factor 1 Complex

Cited by 44 publications

References 30 publications

Transcriptomic and Proteomic Responses of Sweetpotato Whitefly, Bemisia tabaci, to Thiamethoxam

Transcriptomic and Proteomic Responses of Sweetpotato Whitefly, Bemisia tabaci, to Thiamethoxam

Dynamic Changes of the Phosphoproteome in Postmortem Mouse Brains

Functional expansion of human tRNA synthetases achieved by structural inventions

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