scholarly journals The enzymes of human diphosphoinositol polyphosphate metabolism

FEBS Journal ◽  
2013 ◽  
Vol 281 (1) ◽  
pp. 14-33 ◽  
Author(s):  
Mark P. Thomas ◽  
Barry V. L. Potter
Keyword(s):  
Diphosphoinositol Polyphosphate ◽  
Polyphosphate Metabolism

Myo-inositol Polyphosphate Metabolism and Signaling in Arabidopsis

2013 ◽  
Vol 48 (1) ◽  
pp. 94-106
Author(s):  
Wu Li ◽  
Wang Ruozhong ◽  
Xu Wenzhong
Keyword(s):  
Inositol Polyphosphate ◽  
Polyphosphate Metabolism

Dynamics of phosphorus and organic substrates in anaerobic and aerobic phases of a sequencing batch reactor

1994 ◽  
Vol 30 (6) ◽  
pp. 237-246 ◽  
Author(s):  
A. Carucci ◽  
M. Majone ◽  
R. Ramadori ◽  
S. Rossetti
Keyword(s):  
Sequencing Batch Reactor ◽  
Municipal Wastewater ◽  
Batch Reactor ◽  
General Assumption ◽  
Organic Substrate ◽  
Operating Conditions ◽  
Phosphate Removal ◽  
Substrate Uptake ◽  
Organic Substrates ◽  
Polyphosphate Metabolism

This paper describes a lab-scale experimentation carried out to study enhanced biological phosphate removal (EBPR) in a sequencing batch reactor (SBR). The synthetic feed used was based on peptone and glucose as organic substrate to simulate the readily biodegradable fraction of a municipal wastewater (Wentzel et al., 1991). The experimental work was divided into two runs, each characterized by different operating conditions. The phosphorus removal efficiency was considerably higher in the absence of competition for organic substrate between P-accumulating and denitrifying bacteria. The activated sludge consisted mainly of peculiar microorganisms recently described by Cech and Hartman (1990) and called “G bacteria”. The results obtained seem to be inconsistent with the general assumption that the G bacteria are characterized by anaerobic substrate uptake not connected with any polyphosphate metabolism. Supplementary anaerobic batch tests utilizing glucose, peptone and acetate as organic substrates show that the role of acetate in the biochemical mechanisms promoting EBPR may not be so essential as it has been assumed till now.

scholarly journals Copper influence on polyphosphate metabolism of Cunninghamella elegans

2005 ◽  
Vol 36 (4) ◽  
Author(s):  
Patrícia Mendes de Souza ◽  
Petrusk Homero Marinho ◽  
Marcos Antônio Barbosa de Lima ◽  
Aline Elesbão do Nascimento ◽  
Galba Maria de Campos Takaki
Keyword(s):  
Cunninghamella Elegans ◽  
Polyphosphate Metabolism

Genetic Interaction between Ribosome Biogenesis and Inositol Polyphosphate Metabolism inSaccharomyces cerevisiae

2009 ◽  
Vol 73 (2) ◽  
pp. 443-446 ◽  
Author(s):  
Chihiro HORIGOME ◽  
Ryo IKEDA ◽  
Takafumi OKADA ◽  
Kazuhiko TAKENAMI ◽  
Keiko MIZUTA
Keyword(s):  
Ribosome Biogenesis ◽  
Genetic Interaction ◽  
Inositol Polyphosphate ◽  
Polyphosphate Metabolism

scholarly journals Xenotropic and polytropic retrovirus receptor 1 regulates procoagulant platelet polyphosphate

Blood ◽  
2020 ◽  
Author(s):  
Reiner K. Mailer ◽  
Mikel Allende ◽  
Marco Heestermans ◽  
Michaela Schweizer ◽  
Carsten Deppermann ◽  
...  
Keyword(s):  
Arterial Thrombosis ◽  
Gene Deletion ◽  
Thrombus Formation ◽  
Mammalian Species ◽  
Factor Xii ◽  
Phosphate Homeostasis ◽  
Mrna And Protein Expression ◽  
Polyphosphate Accumulation ◽  
Polyphosphate Metabolism

Polyphosphate is a procoagulant inorganic polymer of linear linked orthophosphate residues. Multiple investigations have established the importance of platelet polyphosphate in blood coagulation, however the mechanistic details of polyphosphate homeostasis in mammalian species remain largely undefined. Here, we show that xenotropic and polytropic retrovirus receptor 1 (XPR1) regulates polyphosphate in platelets and is implicated in thrombosis in vivo. We used bioinformatic analyses of omics data to identify XPR1 as a major phosphate transporter in platelets. Xpr1 mRNA and protein expression inversely correlated with intracellular polyphosphate content and release. Pharmacological interference with XPR1 activity increased polyphosphate stores, led to enhanced platelet-driven coagulation and amplified thrombus formation under flow via the polyphosphate/factor XII pathway. Conditional gene deletion of Xpr1 in platelets resulted in polyphosphate accumulation, accelerated arterial thrombosis, and augmented activated platelet-driven pulmonary embolism without increasing bleeding in mice. These data identify platelet XPR1 as an integral regulator of platelet polyphosphate metabolism highlighting a fundamental role for phosphate homeostasis in thrombosis.

scholarly journals Development of a yeast model to study the contribution of vacuolar polyphosphate metabolism to lysine polyphosphorylation

2019 ◽  
Vol 295 (6) ◽  
pp. 1439-1451 ◽  
Author(s):  
Cristina Azevedo ◽  
Yann Desfougères ◽  
Yannasittha Jiramongkol ◽  
Hamish Partington ◽  
Sasanan Trakansuebkul ◽  
...  
Keyword(s):  
Cell Lysis ◽  
Covalent Attachment ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Target Domain ◽  
Inorganic Polyphosphate ◽  
Topoisomerase 1 ◽  
Lysine Residues ◽  
Polyphosphate Metabolism ◽  
Nuclear Targets

A recently-discovered protein post-translational modification, lysine polyphosphorylation (K-PPn), consists of the covalent attachment of inorganic polyphosphate (polyP) to lysine residues. The nonenzymatic nature of K-PPn means that the degree of this modification depends on both polyP abundance and the amino acids surrounding the modified lysine. K-PPn was originally discovered in budding yeast (Saccharomyces cerevisiae), in which polyP anabolism and catabolism are well-characterized. However, yeast vacuoles accumulate large amounts of polyP, and upon cell lysis, the release of the vacuolar polyP could nonphysiologically cause K-PPn of nuclear and cytosolic targets. Moreover, yeast vacuoles possess two very active endopolyphosphatases, Ppn1 and Ppn2, that could have opposing effects on the extent of K-PPn. Here, we characterized the contribution of vacuolar polyP metabolism to K-PPn of two yeast proteins, Top1 (DNA topoisomerase 1) and Nsr1 (nuclear signal recognition 1). We discovered that whereas Top1-targeting K-PPn is only marginally affected by vacuolar polyP metabolism, Nsr1-targeting K-PPn is highly sensitive to the release of polyP and of endopolyphosphatases from the vacuole. Therefore, to better study K-PPn of cytosolic and nuclear targets, we constructed a yeast strain devoid of vacuolar polyP by targeting the exopolyphosphatase Ppx1 to the vacuole and concomitantly depleting the two endopolyphosphatases (ppn1Δppn2Δ, vt-Ppx1). This strain enabled us to study K-PPn of cytosolic and nuclear targets without the interfering effects of cell lysis on vacuole polyP and of endopolyphosphatases. Furthermore, we also define the fundamental nature of the acidic amino acid residues to the K-PPn target domain.

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