Metal binding and conformational studies of the calcium binding domain of NADPH oxidase 5 reveal its similarity and difference to calmodulin

Wei, Chin‐Chuan; Fabry, Emily; Hay, Evan; Lloyd, Laura; Kaufman, Nichole E. M.; Yang, Yaping; Stuehr, Dennis J.

doi:10.1080/07391102.2019.1633409

Cited by 5 publications

(4 citation statements)

References 59 publications

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“…This seems contradictory with previous studies which reported Mg 2+ binding to NOX5‐EF3 . However, these studies used a higher ion concentration ( K a = 4 mM) and reported only minute changes of the structure . It is thus possible that Mg 2+ weakly bind NOX5‐EF3 but it cannot anyway trigger the holo state formation and enzyme activation.…”

Section: Discussioncontrasting

confidence: 60%

“…The C‐lobe is instead disordered in the absence of calcium but acquires a structure in the holo state. Accordingly, a recent study reported that the C‐lobe is less stable than the N‐lobe but has a higher affinity for calcium . Consequently, our studies show that the C‐lobe drives the calcium‐induced conformational change of the EF‐domain of NOX5.…”

Section: Discussionsupporting

confidence: 56%

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On the mechanism of calcium‐dependent activation of NADPH oxidase 5 (NOX5)

et al. 2019

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It is now accepted that reactive oxygen species (ROS) are not only dangerous oxidative agents but also chemical mediators of the redox cell signaling and innate immune response. A central role in ROS‐controlled production is played by the NADPH oxidases (NOXs), a group of seven membrane‐bound enzymes (NOX1‐5 and DUOX1‐2) whose unique function is to produce ROS. Here, we describe the regulation of NOX5, a widespread family member present in cyanobacteria, protists, plants, fungi, and the animal kingdom. We show that the calmodulin‐like regulatory EF‐domain of NOX5 is partially unfolded and detached from the rest of the protein in the absence of calcium. In the presence of calcium, the C‐terminal lobe of the EF‐domain acquires an ordered and more compact structure that enables its binding to the enzyme dehydrogenase (DH) domain. Our spectroscopic and mutagenesis studies further identified a set of conserved aspartate residues in the DH domain that are essential for NOX5 activation. Altogether, our work shows that calcium induces an unfolded‐to‐folded transition of the EF‐domain that promotes direct interaction with a conserved regulatory region, resulting in NOX5 activation.

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Section: Discussioncontrasting

confidence: 60%

Section: Discussionsupporting

confidence: 56%

On the mechanism of calcium‐dependent activation of NADPH oxidase 5 (NOX5)

et al. 2019

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“…Most Ca 2+ receptor proteins contain helix-loop-helix fold (EFhand) motifs that act as Ca 2+ -binding domains. In higher plants, the calcium receptor proteins can be divided into four categories (Wei et al 2019): Calmodulin (CaM), CaM-like proteins (CML), calcineurin B-like proteins (CBL), and calcium-dependent protein kinases (CDPK) (Ma et al 2014), all of which contain EF-hand motifs.…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification and expression analysis of the GhIQD gene family in upland cotton (Gossypium hirsutum L.)

Liu

Kang

et al. 2021

J Cotton Res

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Background Calmodulin (CaM) is one of the most important Ca2+ signaling receptors because it regulates diverse physiological and biochemical reactions in plants. CaM functions by interacting with CaM-binding proteins (CaMBPs) to modulate Ca2+ signaling. IQ domain (IQD) proteins are plant-specific CaMBPs that bind to CaM by their specific CaM binding sites. Results In this study, we identified 102 GhIQD genes in the Gossypium hirsutum L. genome. The GhIQD gene family was classified into four clusters (I, II, III, and IV), and we then mapped the GhIQD genes to the G. hirsutum L. chromosomes. Moreover, we found that 100 of the 102 GhIQD genes resulted from segmental duplication events, indicating that segmental duplication is the main force driving GhIQD gene expansion. Gene expression pattern analysis showed that a total of 89 GhIQD genes expressed in the elongation stage and second cell wall biosynthesis stage of the fiber cells, suggesting that GhIQD genes may contribute to fiber cell development in cotton. In addition, we found that 20 selected GhIQD genes were highly expressed in various tissues. Exogenous application of MeJA significantly enhanced the expression levels of GhIQD genes. Conclusions Our study shows that GhIQD genes are involved in fiber cell development in cotton and are also widely induced by MeJA. Thw results provide bases to systematically characterize the evolution and biological functions of GhIQD genes, as well as clues to breed better cotton varieties in the future.

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“…Calcium receptors proteins in higher plants could be divided into four groups. Helix loop helix fold motif (EF hand motif) was observed in calcium receptors that behave as calcium binding domains (Wei et al 2019).…”

Section: Introductionmentioning

confidence: 99%

Genome Wide Identification, Classification and Functional Characterization of IQD Gene Family in Diploid and Tetraploid Cotton (Gossypium)

Rehman¹,

Peng²,

Li³

et al. 2021

Preprint

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AimsCalmodulin (CaM) is considered as the most significant Ca+ signaling messenger that mediate various biochemical and physiological reactions. Whereas the calcium level can by provoked by extracellular or intracellular stimuli. CaM is activated by calcium binding proteins (CaMBPs) to regulate physiology of the cell. IQ domain (IQD) proteins are plant specific CML/CaM calcium binding which are characterized by domains of 67 amino acids. MethodsHerein, we accomplished a genome wide comparison and analysis of IQD gene family with in two diploid and tetraploid cotton species. Conserved motifs, gene structure, chromosomal map, evolutionary tree, Ka/Ks distribution, promotor analysis, venn diagram for orthologues genes, and collinearity analysis within genome and between genomes of IQD gene family in four cotton species were performed first time. Expression analysis was performed in four species of cotton from SRA database of NCBI.Results293 nonredundant IQD genes were identified from G. arboreum (A2), G. raimondii (D5), G. barbadense (AD2) and G. hirsutum (AD1) and clustered in the reference genomes from cotton functional genomics database. 50, 50, 94, and 99 IQD genes were detected from G. arboreum, G. raimondii, G. barbadense and G. hirsutum respectively. IQD gene family in four species of cotton elucidated the role of allopolyploid and hybridization during evolutionary cascade of allotetraploid cotton. Comparatively, existence of more orthologous genes in cotton species than Arabidopsis, advocated that polyploidization produced new cotton specific orthologous gene clusters. Duplication of gene events depicts that IQD gene family of cotton evolution was under strong purifying selection. G. hirsutum exhibited high level synteny. Expression analysis revealed that GarIQD18, GarIQD25 and GarIQD50 exhibited up regulated expression trend in ovule and fiber in G. arboreum. GarIQD25 also exhibited high expression in stem, root and flower. In G. raimondii, GraIQD03 demonstrated upregulation expression across stem, ovule, fiber and seed. GbaIQD11 and GbaIQD62 exhibited upregulation fiber development in G. barbadense. GhiIQD69 recognized as main candidate genes for plant parts, floral tissues, fiber and ovule development. Promotor analysis identified cis-regulatory elements which are involved in plant defense and stress response mechanisms. ConclusionsOverwhelmingly, present study paves the way to better understand the evolution of cotton IQD genes and lays a foundation for future investigation of IQD genes in improving abiotic stress tolerance in cotton.

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Metal binding and conformational studies of the calcium binding domain of NADPH oxidase 5 reveal its similarity and difference to calmodulin

Cited by 5 publications

References 59 publications

On the mechanism of calcium‐dependent activation of NADPH oxidase 5 (NOX5)

On the mechanism of calcium‐dependent activation of NADPH oxidase 5 (NOX5)

Genome-wide identification and expression analysis of the GhIQD gene family in upland cotton (Gossypium hirsutum L.)

Genome Wide Identification, Classification and Functional Characterization of IQD Gene Family in Diploid and Tetraploid Cotton (Gossypium)

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Metal binding and conformational studies of the calcium binding domain of NADPH oxidase 5 reveal its similarity and difference to calmodulin

Cited by 5 publications

References 59 publications

On the mechanism of calcium‐dependent activation of NADPH oxidase 5 (NOX5)

On the mechanism of calcium‐dependent activation of NADPH oxidase 5 (NOX5)

Genome-wide identification and expression analysis of the GhIQD gene family in upland cotton (Gossypium hirsutum L.)

Genome Wide Identification, Classification and Functional Characterization&nbsp;of IQD Gene Family in Diploid and Tetraploid Cotton (Gossypium)

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Genome Wide Identification, Classification and Functional Characterization of IQD Gene Family in Diploid and Tetraploid Cotton (Gossypium)