Functional analysis of four Class III peroxidases from Chinese pear fruit: a critical role in lignin polymerization

Abstract Background Class III peroxidases (POD) proteins are widely present in the plant kingdom that are involved in a broad range of physiological processes including stress responses and lignin polymerization throughout the plant life cycle. At present, POD genes have been studied in Arabidopsis, rice, poplar, maize and Chinese pear, but there are no reports on the identification and function of POD gene family in Betula pendula. Results We identified 90 nonredundant POD genes in Betula pendula. (designated BpPODs). According to phylogenetic relationships, these POD genes were classified into 12 groups. The BpPODs are distributed in different numbers on the 14 chromosomes, and some BpPODs were located sequentially in tandem on chromosomes. In addition, we analyzed the conserved domains of BpPOD proteins and found that they contain highly conserved motifs. We also investigated their expression patterns in different tissues, the results showed that some BpPODs might play an important role in xylem, leaf, root and flower. Furthermore, under low temperature conditions, some BpPODs showed different expression patterns at different times. Conclusions The research on the structure and function of the POD genes in Betula pendula plays a very important role in understanding the growth and development process and the molecular mechanism of stress resistance. These results lay the theoretical foundation for the genetic improvement of Betula pendula.

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Biochemical and molecular evidence for the role of class III peroxidases in the resistance of carnation (Dianthus caryophyllus L) to Fusarium oxysporum f. sp. dianthi

Physiological and Molecular Plant Pathology ◽

10.1016/j.pmpp.2014.01.003 ◽

2014 ◽

Vol 85 ◽

pp. 42-52 ◽

Cited By ~ 4

Author(s):

Harold Duban Ardila ◽

Angelica María Torres ◽

Sixta Tulia Martínez ◽

Blanca Ligia Higuera

Keyword(s):

Fusarium Oxysporum ◽

Dianthus Caryophyllus ◽

Molecular Evidence ◽

Class Iii ◽

Class Iii Peroxidases

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Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Journal of Biological Chemistry ◽

10.1074/jbc.m402384200 ◽

2004 ◽

Vol 279 (37) ◽

pp. 39000-39009 ◽

Cited By ~ 37

Author(s):

Roberta Pierattelli ◽

Lucia Banci ◽

Nigel A. J. Eady ◽

Jacques Bodiguel ◽

Jamie N. Jones ◽

...

Keyword(s):

Class I ◽

Class Iii ◽

Class Iii Peroxidases

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A Critical Region in the FlaA Flagellin Facilitates Filament Formation of theVibrio choleraeFlagellum

Journal of Bacteriology ◽

10.1128/jb.00029-18 ◽

2018 ◽

Vol 200 (15) ◽

Cited By ~ 8

Author(s):

Mylea A. Echazarreta ◽

Johnathan L. Kepple ◽

Li-Hua Yen ◽

Yue Chen ◽

Karl E. Klose

Keyword(s):

Diarrheal Disease ◽

Critical Role ◽

The Other ◽

Class Iii ◽

Content Type ◽

Important Region ◽

Filament Structure ◽

Flagellar Filament ◽

Necessary And Sufficient ◽

Class Iv

ABSTRACTVibrio choleraeis a Gram-negative bacterium with a monotrichous flagellum that causes the human disease cholera. Flagellum-mediated motility is an integral part of the bacterial life cycle inside the host and in the aquatic environment. TheV. choleraeflagellar filament is composed of five flagellin subunits (FlaA, FlaB, FlaC, FlaD, and FlaE); however, only FlaA is necessary and sufficient for filament synthesis.flaAis transcribed from a class III flagellar promoter, whereas the other four flagellins are transcribed from class IV promoters. However, expressingflaAfrom a class IV promoter still facilitated motility in a strain that was otherwise lacking all five flagellins (ΔflaA-E). Furthermore, FlaA fromV. parahaemolyticus(FlaAVP; 77% identity) supported motility of theV. choleraeΔflaA-Estrain, whereas FlaA fromV. vulnificus(FlaAVV; 75% identity) did not, indicating that FlaA amino acid sequence is responsible for its critical role in flagellar synthesis. Chimeric proteins composed of different domains of FlaAVCand FlaD or FlaAVVrevealed that the N-terminal D1domain (D1N) contains an important region required for FlaA function. Further analyses of chimeric FlaAVC-FlaD proteins identified a lysine residue present at position 145 of the other flagellins but absent from FlaAVCthat can prevent monofilament formation. Moreover, the D1Nregion of amino acids 87 to 153 of FlaAVVinserted into FlaAVCallows monofilament formation but not motility, apparently due to the lack of filament curvature. These results identify residues within the D1Ndomain that allow FlaAVCto fold into a functional filament structure and suggest that FlaAVCassists correct folding of the other flagellins.IMPORTANCEV. choleraecauses the severe diarrheal disease cholera. Its ability to swim is mediated by rotation of a polar flagellum, and this motility is integral to its ability to cause disease and persist in the environment. The current studies illuminate how one specific flagellin (FlaA) within a multiflagellin structure mediates formation of the flagellar filament, thus allowingV. choleraeto swim. This knowledge can lead to safer vaccines and potential therapeutics to inhibit cholera.

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Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions

International Journal of Molecular Sciences ◽

10.3390/ijms19102876 ◽

2018 ◽

Vol 19 (10) ◽

pp. 2876 ◽

Cited By ~ 9

Author(s):

Sabine Lüthje ◽

Teresa Martinez-Cortes

Keyword(s):

Plasma Membranes ◽

Secretory Pathway ◽

In Silico Analysis ◽

Class Iii ◽

Membrane Repair ◽

Protein Protein Interaction ◽

Thale Cress ◽

Membrane Bound ◽

Class Iii Peroxidases ◽

Detergent Resistant Membrane

Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics.

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Class III Peroxidases

Methods in Molecular Biology - Plant Proteomics ◽

10.1007/978-1-62703-631-3_48 ◽

2013 ◽

pp. 687-706 ◽

Cited By ~ 7

Author(s):

Sabine Lüthje ◽

Claudia-Nicole Meisrimler ◽

David Hopff ◽

Tim Schütze ◽

Jenny Köppe ◽

...

Keyword(s):

Class Iii ◽

Class Iii Peroxidases

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Functional analysis of tumour necrosis factor-α-related apoptosis-inducing ligand (TRAIL): cysteine-230 plays a critical role in the homotrimerization and biological activity of this novel tumoricidal cytokine

Biochemical Journal ◽

10.1042/0264-6021:3500505 ◽

2000 ◽

Vol 350 (2) ◽

pp. 505 ◽

Cited By ~ 9

Author(s):

Danyah TRABZUNI ◽

Konrad S. FAMULSKI ◽

Manzoor AHMAD

Keyword(s):

Functional Analysis ◽

Biological Activity ◽

Tumour Necrosis Factor ◽

Tumour Necrosis ◽

Critical Role ◽

Tumour Necrosis Factor Α ◽

Factor Α ◽

Necrosis Factor

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Analysis of Arabidopsis thaliana Redox Gene Network Indicates Evolutionary Expansion of Class III Peroxidase in Plants

Scientific Reports ◽

10.1038/s41598-019-52299-y ◽

2019 ◽

Vol 9 (1) ◽

Cited By ~ 5

Author(s):

Raffael Azevedo de Carvalho Oliveira ◽

Abraão Silveira de Andrade ◽

Danilo Oliveira Imparato ◽

Juliana Gabriela Silva de Lima ◽

Ricardo Victor Machado de Almeida ◽

...

Keyword(s):

Gene Network ◽

Redox System ◽

Plant Evolution ◽

Evolutionary Origin ◽

Class Iii ◽

Ros Metabolism ◽

History Of ◽

Thiol Redox ◽

Public Repositories ◽

Class Iii Peroxidases

Abstract Reactive oxygen species (ROS) are byproducts of aerobic metabolism and may cause oxidative damage to biomolecules. Plants have a complex redox system, involving enzymatic and non-enzymatic compounds. The evolutionary origin of enzymatic antioxidant defense in plants is yet unclear. Here, we describe the redox gene network for A. thaliana and investigate the evolutionary origin of this network. We gathered from public repositories 246 A. thaliana genes directly involved with ROS metabolism and proposed an A. thaliana redox gene network. Using orthology information of 238 Eukaryotes from STRINGdb, we inferred the evolutionary root of each gene to reconstruct the evolutionary history of A. thaliana antioxidant gene network. We found two interconnected clusters: one formed by SOD-related, Thiol-redox, peroxidases, and other oxido-reductase; and the other formed entirely by class III peroxidases. Each cluster emerged in different periods of evolution: the cluster formed by SOD-related, Thiol-redox, peroxidases, and other oxido-reductase emerged before opisthokonta-plant divergence; the cluster composed by class III peroxidases emerged after opisthokonta-plant divergence and therefore contained the most recent network components. According to our results, class III peroxidases are in expansion throughout plant evolution, with new orthologs emerging in each evaluated plant clade divergence.

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