scholarly journals Rice TSV2 Encoding Threonyl-tRNA Synthetase is Needed for Early Chloroplast Development and Seedling Growth under Cold Stress

2021 ◽  
Author(s):  
Dongzhi Lin ◽  
Wenhao Zhou ◽  
Yulu Wang ◽  
Jia Sun ◽  
Xiaobiao Pan ◽  
...  
Keyword(s):  
Cold Stress ◽  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
Trna Synthetase ◽  
Loss Of Function ◽  
Specific Expression ◽  
Trna Synthetases ◽  
Leaf Stage ◽  
Virescent Mutant ◽  
Albino Phenotype

Abstract Threonyl-tRNA synthetase (ThrRS), one of aminoacyl-tRNA synthetases (AARSs), plays a crucial role in protein synthesis. However, the AARS functions on rice chloroplast development and growth were not fully appraised. In this study, a thermo-sensitive virescent mutant tsv2, which showed albino phenotype and lethal after the 4-leaf stage at 20 °C but recovered to normal when the temperatures rose, was identified and characterized. Map-based cloning and complementation tests showed that TSV2 encoded a chloroplast-located ThrRS protein in rice. The Lys-to-Arg mutation in the anticodon-binding domain hampered chloroplast development under cold stress, while the loss-of-function of the ThrRS core domain in TSV2 fatally led to seedling death regardless of growing temperatures. In addition, TSV2 had a specific expression in early leaves. Its disruption obviously resulted in down-regulation of certain genes associated with chlorophyll biosynthesis, photosynthesis and chloroplast development at cold conditions. Our observations revealed that rice nuclear-encoded TSV2 plays an important role in chloroplast development at the early leaf stage under cold stress.

Rice TSV2 Encoding Threonyl-tRNA Synthetase is Needed for Early Chloroplast Development and Seedling Growth under Cold Stress

2020 ◽  
Author(s):  
Dongzhi Lin ◽  
Wenhao Zhou ◽  
Jia Sun ◽  
Yulu Wang ◽  
Xiaobiao Pan ◽  
...  
Keyword(s):  
Plant Growth ◽  
Cold Stress ◽  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
Trna Synthetase ◽  
Loss Of Function ◽  
Specific Expression ◽  
Trna Synthetases ◽  
Virescent Mutant ◽  
Albino Phenotype

Abstract Background The chloroplast is a vital photosynthetic organelle for plant growth and development. However, the genetic factors involved in chloroplast development and its relationship with environment factors are largely unknown. Threonyl-tRNA synthetase (ThrRS), one of aminoacyl-tRNA synthetases (AARSs), plays a crucial role in protein synthesis. To date, there are few studies for AARS function on chloroplast development and plant growth, much less ThrRS in rice. Result In this paper, we characterized a thermo-sensitive virescent mutant tsv2, which showed albino phenotype and could not survive after the 4-leaf stage when grown at 20 °C, but recovered the normal phenotype when the temperature rose. Map-based cloning and complementation tests showed that TSV2 encoded a chloroplast-located ThrRS protein in rice and the Lys-to-Arg mutation in the anticodon-binding domain affected chloroplast development under cold stress. Furthermore, the loss-of-function of the core domain in TSV2 led to seedling death regardless of temperatures. In addition, TSV2 had a tissue-specific expression, and its disruption resulted in an evidently down-regulation of certain genes associated with chlorophyll biosynthesis, photosynthesis and chloroplast development at cold stress. Conclusion The TSV2 encodes a rice threonyl-tRNA synthetase, located in chloroplasts, which is essential for cold-responsive regulation for chloroplast development and plant growth and closely related to the assembly of chloroplast ribosomes and functions at the first step of chloroplast differentiation.

scholarly journals RiceTSV3Encoding Obg-like GTPase Protein is Essential for Chloroplast Development during the Early Leaf Stage under Cold Stress

2017 ◽  
Author(s):  
Dongzhi Lin ◽  
Quan Jiang ◽  
Xiaojing Ma ◽  
Kailun Zheng ◽  
Xiaodi Gong ◽  
...  
Keyword(s):  
Cold Stress ◽  
Chloroplast Development ◽  
Higher Plants ◽  
Complementation Test ◽  
Specific Expression ◽  
Leaf Stage ◽  
Gtp Binding ◽  
Normal Green ◽  
Virescent Mutant ◽  
Higher Temperature

ABSTRACTThe Spo0B-associated GTP-binding (Obg) proteins occupy a wide variety of roles in the viability of nearly all bacteria. Its detailed roles in higher plants have not yet been elucidated. A novel rice thermo-sensitive virescent mutanttsv3was identified in this study that displayed albino phenotype at 20°C before the 3-leaf stage while being normal green at 32°C or even at 20°C after the 4-leaf stage. The mutant phenotype was aligned with altered chlorophyll (Chl) content and chloroplast development. Map-based cloning and complementation test showed thatTSV3encoded a kind of small GTP binding protein. Subcellular localization revealed that TSV3 was in chloroplast.TSV3transcripts were highly expressed in leaves and weak or undetectable in other tissues, suggesting the tissue-specific expression. Intsv3mutant, the transcriptional levels of certain genes associated with biogenesis of chloroplast ribosomes 50S subunit were severely decreased at the 3-leaf-stage under cold stress, but could be recovered to normal levels at a higher temperature (32°C). The observations from this study indicated that the rice nuclear-encodedTSV3plays important roles in chloroplast development at early leaf stage under cold stress.

scholarly journals The Component of the TAC Complex, TCD7, Controls Rice Chloroplast Development at the Early Seedling Stage under Cold Stress

2021 ◽  
Author(s):  
Dongzhi Lin ◽  
Licheng Kang ◽  
Wenhao Zhou ◽  
Yulu Wang ◽  
Yu Chen ◽  
...  
Keyword(s):  
Cold Stress ◽  
Low Temperatures ◽  
Chloroplast Development ◽  
Oryza Sativa L ◽  
Polymerase Activity ◽  
Regulatory Module ◽  
Complex Functions ◽  
In The Wild ◽  
Early Seedling ◽  
Albino Phenotype

Abstract Transcriptionally active chromosome (TAC) is a component of protein-DNA complexes with RNA polymerase activity found in chloroplasts. Although TAC in Arabidopsis thaliana has been extensively investigated, how the rice (Oryza sativa L.) TAC complex functions remains largely unknown. We report the characterization of the mutant thermosensitive chlorophyll-deficient7 (tcd7) and the cloning of TCD7. tcd7 mutant seedlings displayed an albino phenotype specifically at low temperatures and before the four-leaf stage. We identified TCD7 by map-based cloning followed by transgenic rescue and genome editing tests, showing that TCD7 encodes the putative TAC component FRUCTOKINASE-LIKE 2 (OsFLN2). TCD7 transcripts were highly abundant in green tissues, and the protein localized to chloroplasts. In agreement with the albino phenotype, transcript levels of genes controlling chloroplast development and the establishment of photosynthetic capacity were severely reduced in tcd7 seedlings at low temperatures, but were expressed as in the wild type at high temperatures, implying that TCD7 regulates the PEP pathway and chloroplast development. Moreover, TCD7 interacted with the thioredoxin OsTRXz to form an OsTRXz-TCD7 regulatory module, which might regulate plastid transcription under cold stress. Our results demonstrate that the nucleus-encoded TAC protein TCD7 protects chloroplast development from cold stress via a TRXz-FLN regulatory module.

scholarly journals Rice TSV3 Encoding Obg-Like GTPase Protein Is Essential for Chloroplast Development During the Early Leaf Stage Under Cold Stress

2017 ◽  
Vol 8 (1) ◽  
pp. 253-263 ◽  
Author(s):  
Dongzhi Lin ◽  
Quan Jiang ◽  
Xiaojing Ma ◽  
Kailun Zheng ◽  
Xiaodi Gong ◽  
...  
Keyword(s):  
Cold Stress ◽  
Chloroplast Development ◽  
Leaf Stage

Glutamyl and Glutaminyl-tRNA Synthetases Are a Promising Target for the Design of Threonine-Producing Strain

2019 ◽  
Vol 35 (6) ◽  
pp. 39-50
Author(s):  
T.V. Yuzbashev ◽  
A.S. Fedorov ◽  
F.V. Bondarenko ◽  
A.S. Savchenko ◽  
T.V. Vybornaya ◽  
...  
Keyword(s):  
Biomass Accumulation ◽  
Trna Synthetase ◽  
Temperature Sensitive ◽  
Original Strain ◽  
Trna Synthetases ◽  
Resource Center ◽  
Promising Target ◽  
The Russian Federation ◽  
Increase In Productivity ◽  
Culture Growth

The present work describes an approach that improves the properties of the strain producing L-threonine via the reduction in the biomass accumulation during fermentation. Glutamyl- and glutaminyl-tRNA synthetases were chosen as targets. Mutants carrying temperature-sensitive alleles were obtained. It was shown that the used system caused the suppression of the function of tRNA synthetases which led to a rapid arrest of the culture growth, and an increase in productivity and yield of the L-threonine synthesis. One of the temperature-sensitive strains was used to obtain under non-permissive conditions of mutants with the suppressed above phenotype. Some of these mutants accumulate less biomass and produce by 10-12% more threonine than the original strain. Escherichia coli, producing strain, threonine, aminoacyl-tRNA synthetase, ts-mutation This work was supported by the Ministry of Science and Higher Education of the Russian Federation (project code RFMEFI61017X0011), and it was carried out using the equipment of the National Bio-Resource Center All-Russian Collection of Industrial Microorganisms, NRC «Kurchatov Institute» - GosNIIgenetika.

scholarly journals Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Bingyi Chen ◽  
Siting Luo ◽  
Songxuan Zhang ◽  
Yingchen Ju ◽  
Qiong Gu ◽  
...  
Keyword(s):  
Binding Site ◽  
Catalytic Domain ◽  
Trna Synthetase ◽  
Rational Drug Design ◽  
Class I ◽  
Binding Assays ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Rational Drug ◽  
Trna Binding

AbstractThe polyketide natural product reveromycin A (RM-A) exhibits antifungal, anticancer, anti-bone metastasis, anti-periodontitis and anti-osteoporosis activities by selectively inhibiting eukaryotic cytoplasmic isoleucyl-tRNA synthetase (IleRS). Herein, a co-crystal structure suggests that the RM-A molecule occupies the substrate tRNAIle binding site of Saccharomyces cerevisiae IleRS (ScIleRS), by partially mimicking the binding of tRNAIle. RM-A binding is facilitated by the copurified intermediate product isoleucyl-adenylate (Ile-AMP). The binding assays confirm that RM-A competes with tRNAIle while binding synergistically with l-isoleucine or intermediate analogue Ile-AMS to the aminoacylation pocket of ScIleRS. This study highlights that the vast tRNA binding site of the Rossmann-fold catalytic domain of class I aminoacyl-tRNA synthetases could be targeted by a small molecule. This finding will inform future rational drug design.

scholarly journals Lysyl-tRNA synthetase from Escherichia coli K12. Chromatographic heterogeneity and the lysU-gene product

1987 ◽  
Vol 248 (1) ◽  
pp. 43-51 ◽  
Author(s):  
J Charlier ◽  
R Sanchez
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Activity Ratio ◽  
Deae Cellulose ◽  
Trna Synthetase ◽  
Trna Synthetases ◽  
E Coli ◽  
Aminoacyl Trna Synthetases

In contrast with most aminoacyl-tRNA synthetases, the lysyl-tRNA synthetase of Escherichia coli is coded for by two genes, the normal lysS gene and the inducible lysU gene. During its purification from E. coli K12, lysyl-tRNA synthetase was monitored by its aminoacylation and adenosine(5′)tetraphospho(5′)adenosine (Ap4A) synthesis activities. Ap4A synthesis was measured by a new assay using DEAE-cellulose filters. The heterogeneity of lysyl-tRNA synthetase (LysRS) was revealed on hydroxyapatite; we focused on the first peak, LysRS1, because of its higher Ap4A/lysyl-tRNA activity ratio at that stage. Additional differences between LysRS1 and LysRS2 (major peak on hydroxyapatite) were collected. LysRS1 was eluted from phosphocellulose in the presence of the substrates, whereas LysRS2 was not. Phosphocellulose chromatography was used to show the increase of LysRS1 in cells submitted to heat shock. Also, the Mg2+ optimum in the Ap4A-synthesis reaction is much higher for LysRS1. LysRS1 showed a higher thermostability, which was specifically enhanced by Zn2+. These results in vivo and in vitro strongly suggest that LysRS1 is the heat-inducible lysU-gene product.

scholarly journals Notch signaling coordinates ommatidial rotation in the Drosophila eye via transcriptional regulation of the EGF-Receptor ligand Argos

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Yildiz Koca ◽  
Benjamin E. Housden ◽  
William J. Gault ◽  
Sarah J. Bray ◽  
Marek Mlodzik
Keyword(s):  
Notch Signaling ◽  
Cell Fate ◽  
Planar Cell Polarity ◽  
Egf Receptor ◽  
Control Cell ◽  
Loss Of Function ◽  
Egfr Signaling ◽  
Specific Expression ◽  
Egfr Signaling Pathway ◽  
Ommatidial Rotation

AbstractIn all metazoans, a small number of evolutionarily conserved signaling pathways are reiteratively used during development to orchestrate critical patterning and morphogenetic processes. Among these, Notch (N) signaling is essential for most aspects of tissue patterning where it mediates the communication between adjacent cells to control cell fate specification. In Drosophila, Notch signaling is required for several features of eye development, including the R3/R4 cell fate choice and R7 specification. Here we show that hypomorphic alleles of Notch, belonging to the Nfacet class, reveal a novel phenotype: while photoreceptor specification in the mutant ommatidia is largely normal, defects are observed in ommatidial rotation (OR), a planar cell polarity (PCP)-mediated cell motility process. We demonstrate that during OR Notch signaling is specifically required in the R4 photoreceptor to upregulate the transcription of argos (aos), an inhibitory ligand to the epidermal growth factor receptor (EGFR), to fine-tune the activity of EGFR signaling. Consistently, the loss-of-function defects of Nfacet alleles and EGFR-signaling pathway mutants are largely indistinguishable. A Notch-regulated aos enhancer confers R4 specific expression arguing that aos is directly regulated by Notch signaling in this context via Su(H)-Mam-dependent transcription.

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