The Escherichia coli guanosine triphosphate (GTP)-binding proteins Ffh and FtsY have been proposed to catalyze the cotranslational targeting of proteins to the bacterial plasma membrane. A mutation was introduced into the GTP-binding domain of FtsY that altered its nucleotide specificity from GTP to xanthosine triphosphate (XTP). The mutant FtsY protein stimulated GTP hydrolysis by a ribonucleoprotein consisting of Ffh and 4.5S RNA in a reaction that required XTP, and it hydrolyzed XTP in a reaction that required both the Ffh-4.5S ribonucleoprotein and GTP. Thus, nucleotide triphosphate hydrolysis by Ffh and FtsY is likely to occur in reciprocally coupled reactions in which the two interacting guanosine triphosphatases act as regulatory proteins for each other. ...
GUANOSINE TRIPHOSPHATE | C10H16N5O14P3 | CID 6830 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
Proteins that hydrolyze guanine triphosphate to yield guanine diphosphate. This is a class of proteins that belongs to a family of high energy phosphate hydrolases. Members of this family play major roles in biological signal transduction pathways.
Initiation factor 2 (IF-2) is one of the three factors required for the initiation of protein biosynthesis in bacteria [PUBMED:15755955]. IF-2 promotes the GTP-dependent binding of the initiator tRNA to the small subunit of the ribosome. IF-2 is a protein of about 70 to 95 kDa that contains a central GTP-binding domain flanked by a highly variable N-terminal domain and a more conserved C-terminal domain. Some members of this group undergo protein self splicing that involves a post-translational excision of the intein followed by peptide ligation.. ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Guanosine triphosphate, labeled on the alpha phosphate group with 32P, is typically used in reactions involving enzymes that will incorporate the ribonucleoside monophosphate (base, sugar, and alpha-labeled phosphate) into a chain of RNA. Common applications include:. ...
Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. [provided by RefSeq, Jul 2008 ...
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1. Guanosine 5′-[gamma-thio]triphosphate (GTP[S]), if added before GTP, blocks both Ca2+ efflux promoted by GTP and the effect of GTP on enhancement of inositol 1,4,5-triphosphate (IP3)-promoted Ca2+ release from preloaded microsomal vesicles. If, however, GTP[S] is added after GTP, it does not reverse the Ca2+ efflux promoted by GTP, nor does it inhibit IP3-promoted Ca2+ release. 2. The effect of GTP in enhancing IP3-promoted Ca2+ release is maintained after washing the microsomal vesicles free of added GTP. After this treatment, enhancement of IP3-promoted Ca2+ efflux can be observed in the absence of poly(ethylene glycol). 3. Electron microscopy shows that during GTP treatment of microsomal vesicles there is rapid production of very large vesicular structures, apparently produced by fusion of smaller vesicles. 4. Light-scattering changes are detectable during the fusion process. 5. Both Ca2+ efflux promoted by GTP and the enhancement of IP3-promoted Ca2+ release seen in the presence of GTP ...
It has been debated whether the potassium channel of the atrium is activated by the alpha subunit or by the beta gamma subunits of guanine nucleotide binding (G) proteins, which dissociate on activation with guanosine triphosphate (GTP). Therefore, the channel-activating effectiveness of these subunits on isolated guinea pig atrial cells was tested. The activated alpha K subunit from human erythrocytes activated the channel in subpicomolar concentrations. The beta gamma dimer from bovine brain activated the channel in nanomolar concentrations. These results support the view that, physiologically, the alpha subunit activates the channel. ...
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Nagata K et al. (1989) Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein.. ...
Guanine nucleotide-binding proteins (G proteins) ares involved as modulators or transducers in various transmembranes signaling ...
2. Ans. is other than B & E. IN the presence of GTP & all the process has -deltaG & the original AA to Prot reaction has been combined with the GTP hydrolysis as its individual deltaG is positive. MOre than that for deltaG to be positive u cant have -deltaH along with +deltaS. Im seeing for more info ...
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TY - JOUR. T1 - Signal transduction by guanine nucleotide binding proteins. AU - Spiegel, Allen M.. PY - 1987/1. Y1 - 1987/1. N2 - High affinity binding of guanine nucleotides and the ability to hydrolyze bound GTP to GDP are characteristics of an extended family of intracellular proteins. Subsets of this family include cytosolic initiation and elongation factors involved in protein synthesis, and cytoskeletal proteins such as tubulin (Hughes S.M. (1981) FEBS Lett. 164, 1-8). A distinct subset of guanine nucleotide binding proteins is membrane-associated; members of this subset include the ras gene products (Ellis R.W. et al. (1981) Nature 292, 506-511) and the heterotrimeric G-proteins (also termed N-proteins) (Gilman A.G. (1984) Cell 36, 577-579). Substantial evidence indicates that G-proteins act as signal transducers by coupling receptors (R) to effectors (E). A similar function has been suggested but not proven for the ras gene products. Known G-proteins include Gs and Gi, the G-proteins ...
The Gtr1 protein of Saccharomyces cerevisiae is a member of the RagA subfamily of the Ras-like small GTPase superfamily. Gtr1 has been implicated in various cellular processes. Particularly, the Switch regions in the GTPase domain of Gtr1 are essential for TORC1 activation and amino acid signaling. Therefore, knowledge about the biochemical activity of Gtr1 is required to understand its mode of action and regulation. By employing tryptophan fluorescence analysis and radioactive GTPase assays, we demonstrate that Gtr1 can adopt two distinct GDP- and GTP-bound conformations, and that it hydrolyses GTP much slower than Ras proteins. Using cysteine mutagenesis of Arginine-37 and Valine-67, residues at the Switch I and II regions, respectively, we show altered GTPase activity and associated conformational changes as compared to the wild type protein and the cysteine-less mutant. The extremely low intrinsic GTPase activity of Gtr1 implies requirement for interaction with activating proteins to support its
The Rac proteins, Rac1 and Rac2, are essential components of the NADPH oxidase system of phagocytes and regulate the actin assembly associated with membrane ruffling. These functions are controlled by the GTP-bound form of Rac. The biochemical interaction between Rac and its only known GDP-dissociation stimulator (termed smgGDS) was characterized. SmgGDS was able to stimulate the incorporation of guanosine 5′-[gamma-thio]-triphosphate GTP[gamma S] into the RhoA, Rac2, Rac1, Rap1A and CDC42Hs GTP-binding proteins, but the activity was greatest toward RhoA and Rac2. Isoprenoid modification of these proteins was not absolutely required for the interaction with smgGDS. Interestingly, the activity of smgGDS toward Rac1 could not be observed in a [3H]GDP/GTP exchange assay under conditions where it stimulated incorporation of GTP[gamma S] into Rac1. We determined that smgGDS prevented the loss of Rac1 activity during the [3H]GDP/GTP exchange assay by demonstrating the ability of smgGDS to inhibit ...
Agonist binding to guanine nucleotide-binding protein (G protein)-coupled receptors in membranes of myeloid differentiated human leukemia (HL-60) cells is inhibited by guanine nucleotides, most potently by the GTP analog guanosine 5-(gamma-thio)triphosphate (GTP gamma S). In order to study whether GTP gamma S formed locally from adenosine 5-(gamma-thio)triphosphate (ATP gamma S) and GDP by nucleoside diphosphokinase has any advantage over exogenously added GTP gamma S in binding to and activating G proteins, regulation of complement component 5a (C5a) binding to its receptors, as well as formation of GTP gamma S, was studied in membranes of HL-60 cells. GTP gamma S added to HL-60 membranes potently inhibited binding of 125I-C5a (IC50 about 3 nM), an effect not influenced by addition of either GDP or ATP gamma S. When HL-60 membranes were incubated with the combination of ATP gamma S and GDP, a marked potentiation (up to 300-fold) of the inhibition caused by either GDP or ATP gamma S alone was ...
The guanosine triphosphate (GTP)-loaded form of the guanosine triphosphatase (GTPase) Ras initiates multiple signaling pathways by binding to various effectors, such as the kinase Raf and phosphatidylinositol 3-kinase (PI3K). Ras activity is increased by guanine nucleotide exchange factors that stimulate guanosine diphosphate release and GTP loading and is inhibited by GTPase-activating proteins that stimulate GTP hydrolysis. KRAS is the most frequently mutated RAS gene in cancer. Here, we report that monoubiquitination of lysine-147 in the guanine nucleotide-binding motif of wild-type K-Ras could lead to enhanced GTP loading. Furthermore, ubiquitination increased the binding of the oncogenic Gly12Val mutant of K-Ras to the downstream effectors PI3K and Raf. Thus, monoubiquitination could enhance GTP loading on K-Ras and increase its affinity for specific downstream effectors, providing a previously unidentified mechanism for Ras activation.. ...
As shown above, the morphology of the mitotic figure of arsenic-treated cells had features found with both Taxol and Colcemid. These observations correlate with recent findings on the three-dimensional structure of tubulin (18) that show that when the GTP binding site is unoccupied, two cysteine residues, Cys-12 and Cys-213, are in close proximity in the three-dimensional structure, separating after GTP binding occurs. Reaction of trivalent arsenic with these vicinal cysteine residues would inactivate the GTP binding site. This is further supported by an earlier finding that two cysteines in tubulin can be cross-linked after the removal of GTP (19) . These features provide a biochemical basis for the action of arsenic as a noncompetitive inhibitor of GTP binding to tubulin. Confirmation of this mechanism is provided by the preventive effect of exogenous GTP (250-750 μm) on myeloid cell cultures (Fig. 2B) ⇓ . As2O3-induced mitotic arrest in K562 cells was completely blocked in the presence of ...
The bacterial homologues of the signal recognition particle (SRP) and its receptor, the Ffh*4.5S RNA ribonucleoprotein complex and the FtsY protein, respectively, form a unique complex in which both Ffh and FtsY act as GTPase activating proteins for one another, resulting in the mutual stimulation of GTP hydrolysis by both proteins. Previous work showed that 4.5S RNA enhances the GTPase activity in the presence of both Ffh and FtsY, but it was not clear how this was accomplished. In this work, kinetic and thermodynamic analyses of the GTPase reactions of Ffh and FtsY have provided insights into the role of 4.5S RNA in the GTPase cycles of Ffh and FtsY. We found that 4.5S RNA accelerates the association between Ffh and FtsY 400-fold in their GTP-bound form, analogous to its 200-fold catalytic effect on Ffh*FtsY association previously observed with the GppNHp-bound form [Peluso, P., et al. (2000) Science 288, 1640-1643]. Further, Ffh-FtsY association is rate-limiting for the observed GTPase ...
In biology, small GTPases are small (20-25 kDa) proteins that bind to guanosine triphosphate (GTP). This family of proteins is homologous to Ras GTPases and also called the Ras superfamily GTPases. Together with heterotrimeric G-proteins they constitute the G-proteins. They are all GTPases and share common features, but small GTPases have slightly different structures and mechanisms of action. A typical G-protein is active when bound to GTP and inactive when bound to GDP (i.e. when the GTP is hydrolyzed to GDP). The GDP can be then replaced by free GTP. Therefore, a G-protein can be switched on and off. GTP hydrolysis is accelerated by GTPase accelating proteins (GAPs), while GTP exchange is catalyzed by Guanine nucleotide exchange factors (GEFs). Activation of a GEF typically activates its cognate G-protein, while activation of a GAP results in inactivation of the cognate G-protein. Small GTPases regulate a wide variety of processes in the cell, including growth, cellular differentiation, cell ...
Small GTP-binding proteins (G proteins) are monomeric G proteins with a low molecular weight of 20 to 40 kDa. A small G protein acts as a molecular switch that cycles between inactive GDP-bound and active GTP-bound forms. Thus far, ,100 small G proteins have been identified in eukaryotes from yeast to humans. The small G proteins in this superfamily are structurally classified into ≥5 families: the Ras, Rho, Rab, Sar/Arf, and Ran families. In general, the Ras family mainly regulates gene expression, the Rho family regulates both cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate intracellular vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization during the cell cycle.1. Multiple downstream effectors of small G proteins, some of them being protein kinases, have been identified. Ras mediates its effect on cell proliferation mainly by activation of its effector Raf to initiate the mitogen-activated protein ...
The cool thing about the paper is the approach they use. There can be loads of potential targets of ppGpp, and loads of proteins will be inhibited by it in vitro. Which ones are the relevant ones? Kriel and colleagues usa a top-down approach: first they get a birds-eye view of starvation by running metabolic and transcriptomic analysis of starved wt and ppGpp0 (i.e. devoid of ppGpp) strains, then identify the ppGpp targets by clustering and pathway analyses, and then follow their predictions up in vitro and an vivo. This is a really powerful approach. ...
G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). When they are bound to GTP, they are on, and, when they are bound to GDP, they are off. G proteins belong to the larger group of enzymes called GTPases.. There are two classes of G proteins. The first function as monomeric small GTPases, while the second function as heterotrimeric G protein complexes. The latter class of complexes is made up of alpha (α), beta (β) and gamma (γ) subunits.[1] In addition, the beta and gamma subunits can form a stable dimeric complex referred to as the beta-gamma complex.. G proteins located within the cell are activated by G protein-coupled receptors (GPCRs) that span the cell ...
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Author: Wittinghofer, Alfred; Genre: Journal Article; Published in Print: 2002-04-01; Title: Diverse mechanims for GTP hydrolysis by GTP-binding proteins
Author: Wittinghofer, Alfred; Genre: Journal Article; Published in Print: 2002-04-01; Title: Diverse mechanims for GTP hydrolysis by GTP-binding proteins
GTP definition, guanosine triphosphate: an ester of guanosine and triphosphoric acid that is an important metabolic cofactor and precursor in the biosynthesis of cyclic GMP. See more.
Microtubule assembly dynamics: an attractive target for anticancer drugs.: Microtubules, composed of alphabeta tubulin dimers, are dynamic polymers of eukaryoti
Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members ...
Our laboratory studies signal transduction systems controlled by heterotrimeric G proteins as well as Ras-related GTPases. The superfamily of GTPases control numerous signaling cascades based upon the regulated binding, hydrolysis, and exchange of guanine nucleotides; GTPases bound to GTP are active in downstream signaling while those bound to GDP are inactive. Mutant GTPases with abnormal GDP/GTP cycling are implicated in numerous human diseases, including cancer. It is our desire to better understand the regulation of heterotrimeric G proteins and Ras-related GTPases at the molecular level with the ultimate goal of using this information to design therapies to correct abnormal signaling mediated by these proteins and thereby treat associated pathologies.. ...
G proteins are trimeric (alpha-beta-gamma) membrane-associated proteins that regulate flow of information from cell surface receptors to a variety of internal metabolic effectors. Interaction of a G protein with its activated receptor promotes exchange of GTP for GDP that is bound to the alpha subunit. The alpha-GTP complex dissociates from the beta-gamma heterodimer so that the subunits, in turn, may interact with and regulate effector molecules (Gilman, 1987 [PubMed 3113327]; summary by Ahmad et al., 1995) [PubMed 7606925].[supplied by OMIM, Nov 2010 ...
Molecular model of G protein bound to guanine triphosphate (GTP). G proteins, or guanine nucleotide binding proteins, are molecular switches involved in signal transduction. - Stock Image C025/1605
GNG12 overexpression lysate, 0.1 mg. Transient overexpression lysate of guanine nucleotide binding protein (G protein), gamma 12 (GNG12)
pep:known chromosome:VEGA66:3:146499807:146505572:1 gene:OTTMUSG00000029572 transcript:OTTMUST00000073335 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Gng5 description:guanine nucleotide binding protein (G protein), gamma 5 subunit ...
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Homo sapiens cDNA FLJ78228 complete cds, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA ...
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THE GDP DEFLATOR IN NIGERIA WAS REPORTED AT 254.42 IN 2009, ACCORDING TO THE INTERNATIONAL MONETARY FUND (IMF). IN 2015, NIGERIA'S GDP DEFLATOR IS EXPECTED TO BE 444.22 INDEX. THE GDP DEFLATOR IS DERIVED BY DIVIDING CURRENT PRICE GDP BY CONSTANT PRICE GDP AND IS CONSIDERED TO BE AN ALTERNATE MEASURE OF INFLATION. PLEASE NOTE: DATA ARE EXPRESSED IN THE BASE YEAR OF EACH COUNTRY'S NATIONAL ACCOUNTS. IN 2009, NIGERIA'S ECONOMY SHARE OF WORLD TOTAL GDP, ADJUSTED BY PURCHASING POWER PARITY, WAS 0.48 PERCENT. IN 2015, NIGERIA'S SHARE OF WORLD TOTAL GDP IS FORECASTED TO BE 0.53 PERCENT. THIS PAGE INCLUDES A CHART, HISTORICAL DATA AND FORECAST FOR NIGERIA'S GDP DEFLATOR.
GTP binding protein (mammalian Ranp homolog) involved in the maintenance of nuclear organization, RNA processing and transport: interacts with Kap121p, Kap123p and Pdr6p (karyophilin betas): Gsp1p homolog that is not required for ...
Remdesivir triphosphate is synthesised by Santiago Lab. We are providing Remdesivir triphosphate in the form of Na+ salt or Et3N+ salt. Purity (LC-MS) 99 %+
Toc34 is an integral protein in the outer chloroplast membrane thats anchored into it by its hydrophobic[48] C-terminal tail.[38][46] Most of the protein, however, including its large guanosine triphosphate (GTP)-binding domain projects out into the stroma.[46]. Toc34s job is to catch some chloroplast preproteins in the cytosol and hand them off to the rest of the TOC complex.[38] When GTP, an energy molecule similar to ATP attaches to Toc34, the protein becomes much more able to bind to many chloroplast preproteins in the cytosol.[38] The chloroplast preproteins presence causes Toc34 to break GTP into guanosine diphosphate (GDP) and inorganic phosphate. This loss of GTP makes the Toc34 protein release the chloroplast preprotein, handing it off to the next TOC protein.[38] Toc34 then releases the depleted GDP molecule, probably with the help of an unknown GDP exchange factor. A domain of Toc159 might be the exchange factor that carry out the GDP removal. The Toc34 protein can then take up ...
TY - JOUR. T1 - Demonstration and Characterization of Opiate Inhibition of the Striatal Adenylate Cyclase. AU - Law, P. Y.. AU - Wu, J.. AU - Koehler, J. E.. AU - Loh, H. H.. PY - 1981/5. Y1 - 1981/5. N2 - Abstract: The conditions in which Leu5‐enkephalin inhibition of striatal adenylate cyclase was observed were defined. It was determined that enkephalin inhibition was dependent on GTP. The apparent Km for GTP in opiate inhibition was determined to be 0.5 and 2 μM when 0.1 mM‐ and 0.5 mM‐ATP were used as substrate. ITP, but not CTP or UTP, could substitute for GTP in the reaction. Though the addition of monovalent cations-Na+,K+, Li+, Cs+, and choline+-stimulated striatal adenylate cyclase activity, enkephalin inhibition of striatal adenylate cyclase did not require Na+ when theophylline was used as the phosphodiesterase inhibitor. Under optimal conditions, i.e., 20 μM‐GTP and 100 mM‐Na+, Leu5‐enkephalin inhibited the striatal adenylate cyclase activity by 23-27%. When the ...
Addresses: Bilgin N, Univ Uppsala, Ctr Biomed, Dept Biochem, Box 576, S-75123 Uppsala, Sweden. Uppsala Univ, Ctr Biomed, Dept Biol Mol, S-75124 Uppsala, Sweden. Inst Biol Struct, F-38027 Grenoble 1, France. DESY, European Mol Biol Lab, D-22603 Hamburg, GeAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14 ...
The time course of cAMP production by S49 cell membranes in the presence of forskolin and a nonhydrolyzable GTP analog can yield information about the regulation of adenylate cyclase by both the inhibitory and stimulatory GTP-binding proteins (Gi and Gs). The time courses are complex and interpretation in terms of the activities of G1 and Gs requires a quantitative hypothesis. We present a general quantitative hypothesis that defines adenylate cyclase as existing in a distribution of two states, active and inactive. Gi and Gs, in their active states, alter the equilibrium of this distribution. Two distinct models are derived based on this hypothesis to accommodate two different proposed mechanisms for the action of Gi to inhibit adenylate cyclase: 1) a direct interaction between Gi and the catalytic subunit of adenylate cyclase and 2) a direct interaction between Gi and Gs. Perturbations of the regulation of adenylate cyclase by pertussis toxin and phorbol ester are simulated and interpreted ...