Cupins: the most functionally diverse protein superfamily?

Dunwell, J. M.; Purvis, Alan; Khuri, Sawsan

doi:10.1016/j.phytochem.2003.08.016

Cited by 498 publications

(503 citation statements)

References 47 publications

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“…Type II MPIs include bifunctional enzymes with MPI and guanosine diphospho-D-mannose pyrophosphorylase (GMP) activities, which are found, for instance, in Pseudomonas aeruginosa and Xanthomonas campestris. These MPIs are involved in a variety of microbial pathways, including Dmannose metabolism and synthesis of surface polysaccharides, including LPS (Dunwell et al, 2000(Dunwell et al, , 2004.…”

Section: Discussionmentioning

confidence: 99%

The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis

et al. 2009

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The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis Azospirillum brasilense is a plant root-colonizing bacterium that exerts beneficial effects on the growth of many agricultural crops. Extracellular polysaccharides of the bacterium play an important role in its interactions with plant roots. The pRhico plasmid of A. brasilense Sp7, also named p90, carries several genes involved in synthesis and export of cell surface polysaccharides. We generated two Sp7 mutants impaired in two pRhico-located genes, noeJ and noeL, encoding mannose-6-phosphate isomerase and GDP-mannose 4,6-dehydratase, respectively. Our results demonstrate that in A. brasilense Sp7, noeJ and noeL are involved in lipopolysaccharide and exopolysaccharide synthesis. noeJ and noeL mutant strains were significantly altered in their outer membrane and cytoplasmic/periplasmic protein profiles relative to the wild-type strain. Moreover, both noeJ and noeL mutations significantly affected the bacterial responses to several stresses and antimicrobial compounds. Disruption of noeL, but not noeJ, affected the ability of the A. brasilense Sp7 to form biofilms. The pleiotropic alterations observed in the mutants could be due, at least partially, to their altered lipopolysaccharides and exopolysaccharides relative to the wild-type.

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Section: Discussionmentioning

confidence: 99%

The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis

et al. 2009

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“…The oxoglutarate-dependent dioxygenase is a novel H 2 O 2 -inducible gene belonging to a very large gene family that is part of the diverse cupin superfamily (27). Plant oxoglutarate-dependent dioxygenases are mainly implicated in the biosynthesis of flavonoids (28) but also various other secondary metabolites, hydroxyproline-rich proteins and gibberellin (29 -32).…”

Section: Molecular Biology Of H 2 O 2 -Induced Cell Deathmentioning

confidence: 99%

Hydrogen Peroxide-induced Cell Death in Arabidopsis: Transcriptional and Mutant Analysis Reveals a Role of an Oxoglutarate-dependent Dioxygenase Gene in the Cell Death Process

Gechev¹,

Minkov

Hille³

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryHydrogen peroxide is a major regulator of plant programmed cell death (PCD) but little is known about the downstream genes from the H 2 O 2 -signaling network that mediate the cell death. To address this question, a novel system for studying H 2 O 2 -induced programmed cell death in Arabidopsis thaliana was used. The catalase inhibitor aminotriazole (AT) reduced the catalase activity and caused endogenous accumulation of hydrogen peroxide that eventually triggered cell death. Microarray analysis with a DNA chip representing 21500 genes and subsequent comparison with other PCD-related expression studies revealed a set of new H 2 O 2 -responsive genes that were highly regulated in a common fashion during different types of PCD. These included an oxoglutaratedependent dioxygenase and various oxidoreductases, the transcription factors Zat11, WRKY75 and NAM, proteasomal components, a heterologous group of genes with diverse functions, and genes encoding proteins with unknown functions. Knockout lines of the oxoglutarate-dependent dioxygenase exhibited significantly reduced death symptoms and chlorophyll loss upon H 2 O 2 -induced cell death, indicating a role for this gene in the cell death network.

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“…ARD belongs to the cupin structural superfamily. Cupins are a functionally diverse group of proteins distinguished by the presence of an antiparallel β-helix (sometimes called a jellyroll) that forms the central feature of the cupin fold (10,11). We previously described a structural model of Ni-containing ARD based on NMR-derived restraints and molecular modeling in the vicinity of the metal center (9) (PDB entry 1M4O), and have recently published a refinement of that structure that included the use of residual dipolar couplings as restraints in the calculations (PDB entry 1ZRR) (12).…”

Section: Introductionmentioning

confidence: 99%

One Protein, Two Enzymes Revisited: A Structural Entropy Switch Interconverts the Two Isoforms of Acireductone Dioxygenase

Goldsmith

Chai

et al. 2006

Journal of Molecular Biology

130

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SummaryAcireductone dioxygenase (ARD) catalyzes different reactions between O 2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni +2 -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe +2 is bound (ARD ′), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe +2 renders the active site of ARD′ inaccessible to standard NMR methods. The structure of ARD′ has been determined using Fe +2 binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD′. ARD′ retains the β-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the β-sandwich and decreases order at the other upon interconversion of ARD and ARD′, causing loss of the C-terminal helix in ARD′ and rearrangements of residues involved in substrate orientation in the active site.

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Cupins: the most functionally diverse protein superfamily?

Cited by 498 publications

References 47 publications

The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis

The Azospirillum brasilense Sp7 noeJ and noeL genes are involved in extracellular polysaccharide biosynthesis

Hydrogen Peroxide-induced Cell Death in Arabidopsis: Transcriptional and Mutant Analysis Reveals a Role of an Oxoglutarate-dependent Dioxygenase Gene in the Cell Death Process

One Protein, Two Enzymes Revisited: A Structural Entropy Switch Interconverts the Two Isoforms of Acireductone Dioxygenase

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