scholarly journals Phenotypes of NUDIX Hydrolases

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Luiza Bianco ◽  
Sakinah Abdul‐Khaliq ◽  
Nicolette Kulakowski ◽  
Thomas Hynes ◽  
Colleen Kane ◽  
...  
Keyword(s):  
Nudix Hydrolases

scholarly journals Insights into the Genome Sequence ofChromobacterium amazonenseIsolated from a Tropical Freshwater Lake

2018 ◽  
Vol 2018 ◽  
pp. 1-10
Author(s):  
Alexandre Bueno Santos ◽  
Patrícia Silva Costa ◽  
Anderson Oliveira do Carmo ◽  
Gabriel da Rocha Fernandes ◽  
Larissa Lopes Silva Scholte ◽  
...  
Keyword(s):  
De Novo ◽  
Genomic Diversity ◽  
Protein Coding ◽  
Biotechnological Potential ◽  
Draft Assembly ◽  
Functional Studies ◽  
Alpha Hemolysin ◽  
Type Iv ◽  
Nudix Hydrolases ◽  
Colicin V

Members of the genusChromobacteriumhave been isolated from geographically diverse ecosystems and exhibit considerable metabolic flexibility, as well as biotechnological and pathogenic properties in some species. This study reports the draft assembly and detailed sequence analysis ofChromobacterium amazonensestrain 56AF. The de novo-assembled genome is 4,556,707 bp in size and contains 4294 protein-coding and 95 RNA genes, including 88 tRNA, six rRNA, and one tmRNA operon. A repertoire of genes implicated in virulence, for example, hemolysin, hemolytic enterotoxins, colicin V, lytic proteins, and Nudix hydrolases, is present. The genome also contains a collection of genes of biotechnological interest, including esterases, lipase, auxins, chitinases, phytoene synthase and phytoene desaturase, polyhydroxyalkanoates, violacein, plastocyanin/azurin, and detoxifying compounds. Importantly, unlike otherChromobacteriumspecies, the 56AF genome contains genes for pore-forming toxin alpha-hemolysin, a type IV secretion system, among others. The analysis of theC. amazonensestrain 56AF genome reveals the versatility, adaptability, and biotechnological potential of this bacterium. This study provides molecular information that may pave the way for further comparative genomics and functional studies involvingChromobacterium-related isolates and improves our understanding of the global genomic diversity ofChromobacteriumspecies.

Versatile physiological functions of the Nudix Hydrolase family in berry development and stress response in grapevine

2020 ◽  
Author(s):  
Zhaoke Wang ◽  
Peipei Wang ◽  
Le Guan ◽  
Muhammad Salman Haider ◽  
Maazullah Nasim ◽  
...  
Keyword(s):  
Stress Response ◽  
Expression Patterns ◽  
Leaf Roll ◽  
Pcr Analysis ◽  
Berry Development ◽  
Abiotic And Biotic Stresses ◽  
Physiological Functions ◽  
Biotic Stresses ◽  
Wide Range ◽  
Nudix Hydrolases

Abstract Background Nudix hydrolases are widely distributed across all classes of organisms and provide the potential capacity to hydrolyze a wide range of organic pyrophosphates. Although Nudix hydrolases are involved in plants detoxification processes in response to abiotic and biotic stresses, the biological functions of Nudix hydrolases remain largely unclear in grapevine. Results A total of 25 putative grapevine Nudix hydrolases ( VvNUDXs ) were identified by bioinformatics analysis and classified into eight subfamilies based to their preferred substrates. Both tandem and segmental duplications were responsible for the evolution and expansion of NUDX gene family in grapevine. To investigate into their regulatory roles of VvNUDX genes during growth and development as well as in response to abiotic and biotic stress in grapevine, the expression patterns were revealed in publicly available microarray data. The spatial and temporal expression patterns of VvNUDX genes indicated that these genes might play important roles in multiple developmental processes. Transcriptome and qRT-PCR analysis exhibited that ten VvNUDX genes were specifically expressed in grapevine berries, suggesting the potential roles in grapevine berry development. Expression and phylogenetic analysis demonstrated that VvNUDX1 and VvNUDX3 might be involved in terpenoid biosynthesis in grapevine. Futhermore, most VvNUDX genes toward the ADP-ribose/NADH were different patterns in response to various abiotic and biotic stresses, such as salinity and drought, as well as different types of biotic treatments, such as Erysiphe necator , Bois Noir phytoplasma and leaf-roll-associated virus-3 (GLRaV-3). Conclusions These results showed that VvNUDX were associated with plant detoxification processes in response to abiotic and biotic stresses, and regulate disease immunity and resistance pathways. The present informations may provide good opportunities to explore the physiological functions of VvNUDX genes in berry development and stress response networks in grapevine.

Role of NUDIX Hydrolases in NAD and ADP-Ribose Metabolism in Mammals

2020 ◽  
Vol 85 (8) ◽  
pp. 883-894
Author(s):  
V. A. Kulikova ◽  
A. A. Nikiforov
Keyword(s):  
Nudix Hydrolases

scholarly journals A Regulatory Role of NAD Redox Status on Flavin Cofactor Homeostasis inS. cerevisiaeMitochondria

2013 ◽  
Vol 2013 ◽  
pp. 1-16 ◽  
Author(s):  
Teresa Anna Giancaspero ◽  
Vittoria Locato ◽  
Maria Barile
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nicotinamide Adenine Dinucleotide ◽  
Flavin Adenine Dinucleotide ◽  
Redox Balance ◽  
Redox Status ◽  
Cellular Redox ◽  
Isolated Mitochondria ◽  
Nudix Hydrolases ◽  
Order Of Magnitude

Flavin adenine dinucleotide (FAD) and nicotinamide adenine dinucleotide (NAD) are two redox cofactors of pivotal importance for mitochondrial functionality and cellular redox balance. Despite their relevance, the mechanism by which intramitochondrial NAD(H) and FAD levels are maintained remains quite unclear inSaccharomyces cerevisiae. We investigated here the ability of isolated mitochondria to degrade externally added FAD and NAD (in both its reduced and oxidized forms). A set of kinetic experiments demonstrated that mitochondrial FAD and NAD(H) destroying enzymes are different from each other and from the already characterized NUDIX hydrolases. We studied here, in some detail, FAD pyrophosphatase (EC 3.6.1.18), which is inhibited by NAD+and NADH according to a noncompetitive inhibition, withKivalues that differ from each other by an order of magnitude. These findings, together with the ability of mitochondrial FAD pyrophosphatase to metabolize endogenous FAD, presumably deriving from mitochondrial holoflavoproteins destined to degradation, allow for proposing a novel possible role of mitochondrial NAD redox status in regulating FAD homeostasis and/or flavoprotein degradation inS. cerevisiae.

scholarly journals Cloning and Characterization of a New Member of the Nudix Hydrolases from Human and Mouse

2000 ◽  
Vol 275 (12) ◽  
pp. 8844-8853 ◽  
Author(s):  
Hanjing Yang ◽  
Malgorzata M. Slupska ◽  
Ying-Fei Wei ◽  
Jennifer H. Tai ◽  
Wendy M. Luther ◽  
...  
Keyword(s):  
Nudix Hydrolases ◽  
Human And Mouse

Purification, crystallization and preliminary X-ray analysis of two nudix hydrolases fromDeinococcus radiodurans

2003 ◽  
Vol 59 (4) ◽  
pp. 737-740 ◽  
Author(s):  
Elizabeth Litzenberger Holbrook ◽  
Ursula Schulze-Gahmen ◽  
Garry W. Buchko ◽  
Shuisong Ni ◽  
Michael A. Kennedy ◽  
...  
Keyword(s):  
X Ray ◽  
Nudix Hydrolases

scholarly journals Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose

2003 ◽  
Vol 370 (2) ◽  
pp. 409-415 ◽  
Author(s):  
Toshihiro YAGI ◽  
Edurne BAROJA-FERNÁNDEZ ◽  
Ryuji YAMAMOTO ◽  
Francisco José MUÑOZ ◽  
Takashi AKAZAWA ◽  
...  
Keyword(s):  
Human Thyroid ◽  
Kinetic Properties ◽  
Nudix Hydrolase ◽  
Sequence Analyses ◽  
Nucleotide Sugar ◽  
E Coli ◽  
Nudix Hydrolases ◽  
Encoding Gene ◽  
Glycogen Biosynthesis

A distinct UDP-glucose (UDPG) pyrophosphatase (UGPPase, EC 3.6.1.45) has been characterized using pig kidney (Sus scrofa). This enzyme hydrolyses UDPG, the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate (G1P) and UMP. Sequence analyses of the purified enzyme revealed that, similar to the case of a nucleotide-sugar hydrolase controlling the intracellular levels of ADP-glucose linked to glycogen biosynthesis in Escherichia coli [Moreno-Bruna, Baroja-Fernández, Muñoz, Bastarrica-Berasategui, Zandueta-Criado, Rodríguez-López, Lasa, Akazawa and Pozueta-Romero (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 8128—8132], UGPPase appears to be a member of the ubiquitously distributed group of nucleotide pyrophosphatases designated Nudix hydrolases. A complete cDNA of the UGPPase-encoding gene, designated UGPP, was isolated from a human thyroid cDNA library and expressed in E. coli. The resulting cells accumulated a protein that showed kinetic properties identical to those of pig UGPPase.

scholarly journals Molecular Characterization of Organelle-Type Nudix Hydrolases in Arabidopsis

2008 ◽  
Vol 148 (3) ◽  
pp. 1412-1424 ◽  
Author(s):  
Takahisa Ogawa ◽  
Kazuya Yoshimura ◽  
Hiroe Miyake ◽  
Kazuya Ishikawa ◽  
Daisuke Ito ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Nudix Hydrolases
Sign in / Sign up

Export Citation Format

Share Document