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At least 1,243 records · Page 69Linked to original sources
PubMed1973

Nonribosomal synthesis of guanosine 5',3'-polyphosphates by the ribosomal wash of stringent Escherichia coli.

A factor in the ribosomal wash of stringent strains of E. coli was identified by Haseltine et al. as a complement to the ribosomal system for the synthesis of the magic spot compounds of Cashel and Gallant. This factor has been found, in the absence of ribosomes, to catalyze the enzymatic pyrophosphoryl transfer from ATP to GTP or GTP in the formation of magic spot I and magic spot II, the guanosine tetra- and pentaphosphates (ppGpp and pppGpp), respectively. The enzyme, which normally requires the presence of the ribosome-tRNA-mRNA complex for activity, catalyzes a very slow synthesis that is stimulated tenfold by 20% methanol. The temperature optimum of the methanol-stimulated system is 25-30 degrees and activity is drastically depressed at 37 degrees , presumably by inactivation. Catalysis is linear with enzyme concentration and with time for the first 3 hr; during this period 25% of the added GTP is converted. The nonribosomal system is distinguished from the ribosomal system by having a lower Mg(++) and a higher NH(4) (+) optimum. The two systems differ in their response to antibiotics: thiostrepton strongly inhibits the ribosomal system but has no effect on the nonribosomal system.

Ammonium Chloride↗
PubMed1996

2',5'-Dideoxyadenosine 3'-polyphosphates are potent inhibitors of adenylyl cyclases.

2',5'-Dideoxyadenosine 3'-di- and triphosphates were tested as inhibitors of brain adenylyl cyclases. With an IC50 approximately 40 nM, 2',5'-dideoxy-3'-ATP is the most potent nonprotein synthetic regulator of adenylyl cyclases thus far described. Neither 2',5'-dideoxy-3'-ADP nor 2',5'-dideoxy-3'-ATP inhibited activity by competition with substrate, and the linear noncompetitive inhibition observed was consistent with interaction via a distinct domain. The availability of this ligand will permit the development of a variety of probes that will be extremely useful in investigating adenylyl cyclase structure and the role(s) that this class of compound may play in physiologically regulating cell function.

Adenylyl Cyclase Inhibitors↗
PubMed2004

Signaling by higher inositol polyphosphates. Synthesis of bisdiphosphoinositol tetrakisphosphate ("InsP8") is selectively activated by hyperosmotic stress.

Evidence has accumulated that inositol pyrophosphates (diphosphoinositol pentakisphosphate (PP-InsP5) and bisdiphosphoinositol tetrakisphosphate ([PP]2-InsP4)) are intracellular signals that regulate many cellular processes including endocytosis, vesicle trafficking, apoptosis, and DNA repair. Yet, in contrast to the situation with all other second messengers, no one studying multicellular organisms has previously described a stimulus that acutely and specifically elevates cellular levels of PP-InsP5 or [PP]2-InsP4. We now show up to 25-fold elevations in [PP]2-InsP4 levels in animal cells. Importantly, this does not involve classical agonists. Instead, we show that this [PP]2-InsP4 response is a novel consequence of the activation of ERK1/2 and p38MAPalpha/beta kinases by hyperosmotic stress. JNK did not participate in regulating [PP]2-InsP4 levels. Identification of [PP]2-InsP4 as a sensor of hyperosmotic stress opens up a new area of research for studies into the cellular activities of higher inositol phosphates.

Animals↗
PubMed2003

Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation.

SKIP (skeletal muscle and kidney enriched inositol phosphatase) is a recently identified phosphatidylinositol 3,4,5-trisphosphate- and phosphatidylinositol 4,5-bisphosphate-specific 5-phosphatase. In this study, we investigated the intracellular localization of SKIP. Indirect immunofluorescence and subcellular fractionation showed that, in serum-starved cells, both endogenous and recombinant SKIP colocalized with markers of the endoplasmic reticulum (ER). Following epidermal growth factor (EGF) stimulation, SKIP transiently translocated to plasma membrane ruffles and colocalized with submembranous actin. Data base searching demonstrated a novel 128-amino acid domain in the C terminus of SKIP, designated SKICH for SKIP carboxyl homology, which is also found in the 107-kDa 5-phosphatase PIPP and in members of the TRAF6-binding protein family. Recombinant SKIP lacking the SKICH domain localized to the ER, but did not translocate to membrane ruffles following EGF stimulation. The SKIP SKICH domain showed perinuclear localization and mediated EGF-stimulated plasma membrane ruffle localization. The SKICH domain of the 5-phosphatase PIPP also mediated plasma membrane ruffle localization. Mutational analysis identified the core sequence within the SKICH domain that mediated constitutive membrane association and C-terminal sequences unique to SKIP that contributed to ER localization. Collectively, these studies demonstrate a novel membrane-targeting domain that serves to recruit SKIP and PIPP to membrane ruffles.

Amino Acid Sequence↗
PubMed2005

Effect of chilling, polyphosphate and bicarbonate on quality characteristics of broiler breast meat.

1. An experiment was conducted to assess the effect of tetrasodium pyrophosphate and sodium bicarbonate on colour and sensory attributes of pre- and post-chilled breast meat. 2. Three groups of 6 halves of breasts (pre-chill) immediately after slaughter were treated with 3% tetrasodium pyrophosphate, 3% sodium bicarbonate in 2% NaCl or 2% NaCl alone (control); the remaining 6 halves (post-chill) were stored overnight at 4 degrees C and then treated similarly. Both the pre- and post-chill samples were held at 4 degrees C for 24 h and pH, water holding capacity, cooking loss, CIE colour values and sensory attributes were recorded. 3. Chilling had few effects on the meat characteristics measured in this study. 4. Treatment with phosphate and bicarbonate increased pH in both the pre- and post-chill groups. Treated breasts exhibited lower L* and higher a* value (more red) than controls. 5. A sensory evaluation study revealed improvements in colour and other sensory attributes of cooked broiler breast meat in all treated samples compared to the control. 6. The findings suggest that tetrasodium pyrophosphate and sodium bicarbonate, when injected post mortem, will have beneficial effects on several physico-chemical (pH, colour, WHC %, cooking loss) and sensory attributes of broiler meat. However, phosphate had a smaller effect than bicarbonate.

Animals↗
PubMed1990

Interaction of purine nucleotides with inert paramagnetic Cr(III) probes evaluated by NMR relaxation effects. Molecular mechanics calculations on Cr(III) and Co(III) polyphosphate complexes.

The 1H NMR relaxation effects produced by paramagnetic Cr(III) complexes on nucleoside 5'-mono- and -triphosphates in D2O solution at pH' = 3 were measured. The paramagnetic probes were [Cr(III)(H2O)6]3+, [Cr(III)(H2O)3(HATP)], [Cr(III)(H2O)3(HCTP)] and [Cr(III)(H2O)3(UTP)-, while the matrix nucleotides (0.1 M) were H2AMP, HIMP-, and H2ATP2-. For the aromatic base protons, the ratios of the transverse to longitudinal paramagnetic relaxation rates (R2p/R1p) for the [Cr(III)(H2O)6]3+/H2ATP2-, [Cr(III)(H2O)3(HATP)]/H2ATP2-, [Cr(III)(H2O)3(HCTP)]/H2ATP2 and [Cr(III)(H2O)3(UTP)]-/H2ATP2 systems were below 2.33 so the dipolar term predominates. For a given nucleotide, R1p for the purine H(8) signal was larger than for the H(2) signal with the [Cr(III)(H2O)6]3+ probe, while R1p for the H(2) signal was larger with all the other Cr(III) probes. Molecular mechanics computations on the [Cr(III)(H2O)4(HPP)(alpha,beta)], [Cr(III)(NH3)4(HPP)(alpha,beta)], [Co(III)(NH3)3(H2PPP)(alpha,beta,gamma)] and [Co(III)(NH3)4(HPP)(alpha,beta)] complexes gave calculated energy-minimized geometries in good agreement with those reported in crystal structures. The molecular mechanics force constants found were then used to calculate the geometry of the inner sphere [Cr(III)(H2O)6]3+ and [Cr(III)(H2O)3(HATP)(alpha,beta,gamma)] complexes as well as the structures of the outer sphere [Cr(III)(H2O)6]3(+)-(H2AMP) and [Cr(III)(H2O)6]-(HIMP)- species. The gas-phase structure of the [Cr(III)(H2O)3(HATP)(alpha,beta,gamma)] complex shows the existence of a hydrogen bond interaction between a water ligand and the adenine N(7)(O...N = 2.82 A). The structure is also stabilized by intramolecular hydrogen bonds involving the -O(2')H group and the adenine N(3) (O...N = 2.80 A) as well as phosphate oxygen atoms and a water molecule (O...O = 2.47 A). The metal center has an almost regular octahedral coordination geometry. The structures of the two outer-sphere species reveal that the phosphate group interacts strongly with the hexa-aquochromium probe. In both complexes, the nucleotides have a similar "anti" conformation around the N(9)-C(1') glycosidic bond. However, a very important difference characterizes the two structures. For the (HIMP)- complex, strong hydrogen bond interactions exist between one and two water ligands and the inosine N(7) and O(6) atoms, respectively (O...O = 2.63 A; O...N = 2.72, 2.70 A). For the H2AMP complex, the [Cr(III)(H2O)6]3+ cation does not interact with N(7) since it is far from the purine system. Hydrogen bonds occur between water ligands and phosphate oxygens. The Cr-H(8) and Cr-H(2) distances revealed by the energy-minimized geometries for the two outer sphere species were used to calculate the R1p values for the H(8) and H(2) signals for comparison with the observed R1p values: 0.92(c), 1.04(ob) (H(8)) and 0.06(c), 0.35(ob) (H(2)) for H2AMP; and 3.76(c), 4.53(ob) (H(8)) and 0.16(c), 0.77(ob) s-1 (H(2)) for HIMP-.(ABSTRACT TRUNCATED AT 400 WORDS)

Chromium↗
PubMed1975

Localized intracellular polyphosphate formation by Desulfovibrio gigas.

The dissimilatory sulphate-reducing bacterium Desulfovibrio gigas, frequently sub-cultured, often contained spherical granules which stained metachromatically with some basic dyes. The granules were examined in situ by transmission electron microscopy of whole organisms and thin sections. The granules were isolated from broken bacteria as a water-insoluble, non-crystalline, white material containing magnesium, phosphorus and organic carbon, but devoid of sulphur and nitrogen. The molar ratio of phosphorus to magnesium (1 to 17) was close to the proportions in magnesium tripolyphosphate. Infrared absorption spectra for the white material and magnesium tripolyphosphate were similar.

Carbon↗
PubMed1983

The role of magnesium in binding of the nucleotide polyphosphate chain to the active site of myosin subfragment-1.

The binding of adenosine 5'-[beta, gamma-imido]triphosphate, pyrophosphate and triphosphate to the active site of myosin subfragment-1 was assessed in the presence and absence of Mg2+ by direct and indirect methods. In addition, the affinity and stoichiometry of Mg2+ in the ternary complexes formed by protein, Mg2+ and each of these phosphate compounds have been determined. As direct methods, equilibrium dialysis, sedimentation and quantitative affinity chromatography were used in conjunction with the indirect method of monitoring reactivity changes of the critical thiol-1 and thiol-2 groups, which occur upon binding of the ligands at the active site. There was good agreement between the results yielded by the different methods. All three phosphate compounds alone bind just one molecule per isolated myosin head portion with similar affinities lying in the range 1-4 X 10(3) M-1. Again only one molecule/head portion binds when they exist in the form complexed with Mg2+, but now show much higher affinities of between 10(6)-10(7) M-1. In all cases Mg2+ was found to be associated in the ternary complexes with the very high affinity of 10(8)-10(9) M-1. It is postulated that this ion plays a prominent role in fixing the phosphate chain in the myosin active site. In contrast, Mg2+ scarcely affects the affinity of ADP and shows only a low affinity around 4 X 10(4) M-1 in the ternary complex [Watterson, J.G., Foletta, D., Kunz, P.A., and Schaub, M. C. (1983) Eur. J. Biochem. 131, 89-96]. As pyrophosphate displays binding parameters similar to the triphosphate compounds and widely different from ADP, it is argued that it may bind in the beta, gamma-phosphate positions at the active site.

Adenine Nucleotides↗