Late embryogenesis abundant group3 protein (DrLEA3) is involved in antioxidation in the extremophilic bacterium Deinococcus radiodurans

Dai, Jingli; Gao, Kaixuan; Yao, Tao; Lu, Haijun; Zhou, Changjiang; Guo, Miao; Dai, Shang; Wang, Liangyan; Xu, Hong; Teng, Bing; Hua, Yuejin; Zhao, Ye

doi:10.1016/j.micres.2020.126559

Cited by 21 publications

(22 citation statements)

References 48 publications

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“…LEAM protein derived from pea ( Pisum sativum ) belongs to the G3LEA family, which interacts with the membrane in the dry state and protects the liposomes subjected to drying [ 22 ]. The DosH protein has also been confirmed to be enriched on the cell membrane and bind to a variety of metal ions in vivo [ 25 ]. These results indicate that the G3LEA proteins may be involved in the stability of cell membrane.…”

Section: Discussionmentioning

confidence: 99%

“…At present, it is known that most G3LEA proteins and their hydrophilic domains (HD) are intrinsically disordered proteins (IDPs) in aqueous solutions, but, when the solution contains SDS, TFE, glycerol, methanol, or is under drought conditions, they become highly ordered α-helix structure [ 22 , 23 , 24 ]. The DosH ( Deinococcus ordered stress-inducible Hydrophilic) protein derived from D. radiodurans belongs to the G3LEA protein family, and its secondary structure determination shows that it contains 45% α-helix, which is a naturally ordered G3LEA protein and involved in the cellular defense against oxidative stress [ 25 ]. Previous research in our laboratory found that the N-terminal domain (position 1–103) of the DosH protein alone does not function, but it is the key region that helps the DosH protein fold into an ordered secondary structure (data not shown).…”

Section: Introductionmentioning

confidence: 99%

“…The following are available online at , Figure S1: Analysis of the order and amino acid composition of the N-terminal domain of DosH protein; Figure S2: Multiple sequence alignment analysis based on DosH protein in Deinococcus ; Figure S3: Hydropathic index plot of recombinant proteins analyzed by using the Kyte-Doolittle algorithm; Figure S4: Catalase activity analysis; Figure S5: Phylogenetic analysis of hydrophilic domains from different organisms; Table S1: The composition of each recombinant protein analyzed by using the ProtParam; Table S2: Secondary structure content in eight recombinant proteins was obtained by far UV CD spectrometry and calculated with CDNN software; Table S3: The characteristics of G3LEA proteins reported; Table S4: Strains and plasmids used in this study; Table S5: List of primers required for construction of recombinant E. coli strain. References [ 8 , 22 , 24 , 25 , 37 , 57 , 58 , 59 , 60 , 61 , 62 , 63 ] are cited in the supplementary materials.…”

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confidence: 99%

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Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Guo

Zhao

Tang

et al. 2021

IJMS

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Most late embryogenesis abundant group 3 (G3LEA) proteins are highly hydrophilic and disordered, which can be transformed into ordered α-helices to play an important role in responding to diverse stresses in numerous organisms. Unlike most G3LEA proteins, DosH derived from Dinococcus radiodurans is a naturally ordered G3LEA protein, and previous studies have found that the N-terminal domain (position 1–103) of DosH protein is the key region for its folding into an ordered secondary structure. Synthetic biology provides the possibility for artificial assembling ordered G3LEA proteins or their analogues. In this report, we used the N-terminal domain of DosH protein as module A (named DS) and the hydrophilic domains (DrHD, BnHD, CeHD, and YlHD) of G3LEA protein from different sources as module B, and artificially assembled four non-natural hydrophilic proteins, named DS + DrHD, DS + BnHD, DS + CeHD, and DS + YlHD, respectively. Circular dichroism showed that the four hydrophile proteins were highly ordered proteins, in which the α-helix contents were DS + DrHD (56.1%), DS + BnHD (53.7%), DS + CeHD (49.1%), and DS + YLHD (64.6%), respectively. Phenotypic analysis showed that the survival rate of recombinant Escherichia coli containing ordered hydrophilic protein was more than 10% after 4 h treatment with 1.5 M NaCl, which was much higher than that of the control group. Meanwhile, in vivo enzyme activity results showed that they had higher activities of superoxide dismutase, catalase, lactate dehydrogenase and less malondialdehyde production. Based on these results, the N-terminal domain of DosH protein can be applied in synthetic biology due to the fact that it can change the order of hydrophilic domains, thus increasing stress resistance.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Guo

Zhao

Tang

et al. 2021

IJMS

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“…Bacterial LEA protein functions have not been extensively studied; however, some LEA_4 proteins play a role in resistance to abiotic stresses. DrLEA3 of Deinococcus radiodurans is involved in desiccation and oxidation tolerance [ 4 , 8 ], and Zmo0994 of Zymomonas mobilis increases tolerance to ethanol [ 9 ]. Some LEA proteins may adopt α-helical structures when water levels decrease [ 67 ], and the α-helical structure of dehydrins, which form a separate dehydrin class in the Pfam LEA classification, interacts electrostatically with lipid membranes [ 68 ].…”

Section: Discussionmentioning

confidence: 99%

Decreased temperature increases the expression of a disordered bacterial late embryogenesis abundant (LEA) protein that enhances natural transformation

et al. 2021

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Late embryogenesis abundant (LEA) proteins are important players in the management of responses to stressful conditions, such as drought, high salinity, and changes in temperature. Many LEA proteins do not have defined three-dimensional structures, so they are intrinsically disordered proteins (IDPs) and are often highly hydrophilic. Although LEA-like sequences have been identified in bacterial genomes, the functions of bacterial LEA proteins have been studied only recently. Sequence analysis of outer membrane interleukin receptor I (BilRI) from the oral pathogen Aggregatibacter actinomycetemcomitans indicated that it shared sequence similarity with group 3/3b/4 LEA proteins. Comprehensive nuclearcgq magnetic resonance (NMR) studies confirmed its IDP nature, and expression studies in A. actinomycetemcomitans harboring a red fluorescence reporter protein-encoding gene revealed that bilRI promoter expression was increased at decreased temperatures. The amino acid backbone of BilRI did not stimulate either the production of reactive oxygen species from human leukocytes or the production of interleukin-6 from human macrophages. Moreover, BilRI-specific IgG antibodies could not be detected in the sera of A. actinomycetemcomitans culture-positive periodontitis patients. Since the bilRI gene is located near genes involved in natural competence (i.e., genes associated with the uptake of extracellular (eDNA) and its incorporation into the genome), we also investigated the role of BilRI in these events. Compared to wild-type cells, the Δ bilRI mutants showed a lower transformation efficiency, which indicates either a direct or indirect role in natural competence. In conclusion, A. actinomycetemcomitans might express BilRI, especially outside the host, to survive under stressful conditions and improve its transmission potential.

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“…Recently, the roles of LEA proteins in D. radiodurans were elaborated in a succession of papers [21] , [22] , [42] , among which three genes encoding LEA family proteins (locus tag DR_1172 , DR_0105 and DR_1372 ) were annotated in the genome of D. radiodurans ( Table 2 ). Thus, DR1172 is rich in hydrophilic amino acids residues, which were clustered to a typical Hydrophilic Domain (HD) with 8 conserved motifs.…”

Section: Characterization Of Lea Proteins In D Radioduransmentioning

confidence: 99%

Pleiotropic roles of late embryogenesis abundant proteins of Deinococcus radiodurans against oxidation and desiccation

Liu

Zhang

Wang

et al. 2021

Computational and Structural Biotechnology Journal

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Deinococcus radiodurans, an important extremophile, possesses extraordinary stress tolerance ability against lethal and mutagenic effects of DNA-damaging agents, such as γ-rays, ultraviolet, oxidation, and desiccation. How global regulators of this bacterium function in response to oxidation and desiccation has been an intense topic as elucidating such mechanisms may help to facilitate some beneficial applications in agriculture or medicine. Particularly, a variety of functional proteins have been characterized for D. radiodurans ’ behaviors under abiotic stresses. Interestingly, a group of L ate E mbryogenesis A bundant proteins (LEAs) in D. radiodurans have been characterized both biochemically and physiologically, which are shown indispensable for stabilizing crucial metabolic enzymes in a chaperone-like manner and thereby maintaining the metal ion homeostasis under oxidation and desiccation. The rapid progress in understanding deinococcal LEA proteins has substantially extended their functions in both plants and animals. Herein, we discuss the latest studies of radiodurans LEA proteins ranging from the classification to structures to functions. Importantly, the harnessing of these proteins may have unlimited potential for biotechnology, engineering and disease treatments.

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Late embryogenesis abundant group3 protein (DrLEA3) is involved in antioxidation in the extremophilic bacterium Deinococcus radiodurans

Cited by 21 publications

References 48 publications

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Decreased temperature increases the expression of a disordered bacterial late embryogenesis abundant (LEA) protein that enhances natural transformation

Pleiotropic roles of late embryogenesis abundant proteins of Deinococcus radiodurans against oxidation and desiccation

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