Contents
Academic literature on the topic 'Mant-ATP'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Mant-ATP.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Mant-ATP"
1
Maruta, S., and M. Ikebe. "Photoaffinity labelling of smooth-muscle myosin by methylanthraniloyl-8-azido-ATP." Biochemical Journal 292, no. 2 (1993): 439–44. http://dx.doi.org/10.1042/bj2920439.
Full textAbstract:
Methylanthraniloyl-8-azido-ATP (Mant-8-N3-ATP), which binds to the 20 kDa C-terminal tryptic fragment of skeletal-muscle myosin subfragment-1 [Maruta, Miyanishi and Matsuda (1989) Eur. J. Biochem. 184, 213-221], was synthesized and used as a probe of the conformational change of smooth-muscle myosin. Mant-8-N3-ATP, like ATP, induced the formation of the 10 S conformation at low ionic strength. In the presence of vanadate, smooth-muscle myosin formed a stable complex with Mant-8-N3-ADP, and this complex showed the 10 S→6 S transition of myosin. ATP-binding sites for 6 S (extended state) and 10 S (folded state) myosin were studied by photolabelling of myosin with Mant-8-N3-ADP. For both 6 S and 10 S myosin, Mant-8-N3-ATP was incorporated into the 29 kDa N-terminal tryptic fragment of myosin heavy chain. This is unlike the labelling of skeletal-muscle myosin, in which the 20 kDa C-terminal fragment is labelled. The labelling of 29 kDa fragment was diminished significantly by addition of ATP. These results suggest that the conformation of the ATP-binding site of smooth-muscle myosin is different from that of skeletal-muscle myosin. To examine further the possible differences in the labelling site between 6 S and 10 S myosin, the affinity-labelled 29 kDa fragment was subjected to complete proteolysis by lysylendo-peptidase. The fluorescent-labelled-peptide map suggested that the Mant-8-N3-ADP-binding sites for 6 S and 10 S myosin were identical.
2
Myburgh, K. H., K. Franks-Skiba, and R. Cooke. "Nucleotide turnover rate measured in fully relaxed rabbit skeletal muscle myofibrils." Journal of General Physiology 106, no. 5 (1995): 957–73. http://dx.doi.org/10.1085/jgp.106.5.957.
Full textAbstract:
Steady state measurements of the ATP turnover rate of myosin crossbridges in relaxed living mammalian muscle or in in vitro systems are complicated by other more rapid ATPase activities. To surmount these problems we have developed a technique to measure the nucleotide turnover rate of fully relaxed myosin heads in myofibrils using a fluorescent analogue of ATP (mant-ATP). Rabbit myofibrils, relaxed in 1.6 mM ATP, were rapidly mixed with an equal volume of solution containing 80 microM mant-ATP and injected into a fluorimeter. As bound ADP is released, a fraction of the myosin active sites bind mant-ATP and fluorescence emission rises exponentially, defining a rate of nucleotide turnover of 0.03 +/- 0.001 s-1 at 25 degrees C (n = 17). This rate was approximately equal to one half that of purified myosin. The turnover rates for myosin and myofibrils increased between 5 degrees and 42 degrees C, reaching 0.16 +/- 0.04 s-1 and 0.06 +/- 0.005 s-1, respectively, at 39 degrees C, the body temperature of the rabbit. If the rate observed for purified myosin occurred in vivo, it would generate more heat than is observed for resting living muscle. When myosin is incorporated into the myofilament lattice, its ATPase activity is inhibited, providing at least a partial explanation for the low rate of heat production by living resting muscle.
3
Szulc, A., D. Appelhans, B. Voit, M. Bryszewska, and B. Klajnert. "Studying Complexes Between PPI Dendrimers and Mant-ATP." Journal of Fluorescence 23, no. 2 (2013): 349–56. http://dx.doi.org/10.1007/s10895-012-1153-y.
Full text
4
Gille, Andreas, Gerald H. Lushington, Tung-Chung Mou, Michael B. Doughty, Roger A. Johnson, and Roland Seifert. "Differential Inhibition of Adenylyl Cyclase Isoforms and Soluble Guanylyl Cyclase by Purine and Pyrimidine Nucleotides." Journal of Biological Chemistry 279, no. 19 (2004): 19955–69. http://dx.doi.org/10.1074/jbc.m312560200.
Full textAbstract:
Mammals express nine membranous adenylyl cyclase isoforms (ACs 1–9), a structurally related soluble guanylyl cyclase (sGC) and a soluble AC (sAC). Moreover,Bacillus anthracisandBacillus pertussisproduce the AC toxins, edema factor (EF), and adenylyl cyclase toxin (ACT), respectively. 2′(3′)-O-(N-methylanthraniloyl)-guanosine 5′-[γ-thio]triphosphate is a potent competitive inhibitor of AC in S49 lymphoma cell membranes. These data prompted us to study systematically the effects of 24 nucleotides on AC in S49 and Sf9 insect cell membranes, ACs 1, 2, 5, and 6, expressed in Sf9 membranes and purified catalytic subunits of membranous ACs (C1 of AC5 and C2 of AC2), sAC, sGC, EF, and ACT in the presence of MnCl2.N-Methylanthraniloyl (MANT)-GTP inhibited C1·C2 with aKiof 4.2 nm. Phe-889 and Ile-940 of C2 mediate hydrophobic interactions with the MANT group. MANT-inosine 5′-[γ-thio]triphosphate potently inhibited C1·C2 and ACs 1, 5, and 6 but exhibited only low affinity for sGC, EF, ACT, and G-proteins. Inosine 5′-[γ-thio]triphosphate and uridine 5′-[γ-thio]triphosphate were mixed G-protein activators and AC inhibitors. AC5 was up to 15-fold more sensitive to inhibitors than AC2. EF and ACT exhibited unique inhibitor profiles. At sAC, 2′,5′-dideoxyadenosine 3′-triphosphate was the most potent compound (IC50, 690 nm). Several MANT-adenine and MANT-guanine nucleotides inhibited sGC withKivalues in the 200–400 nmrange. UTP and ATP exhibited similar affinities for sGC as GTP and were mixed sGC substrates and inhibitors. The exchange of MnCl2against MgCl2reduced inhibitor potencies at ACs and sGC 1.5–250-fold, depending on the nucleotide and cyclase studied. The omission of the NTP-regenerating system from cyclase reactions strongly reduced the potencies of MANT-ADP, indicative for phosphorylation to MANT-ATP by pyruvate kinase. Collectively, AC isoforms and sGC are differentially inhibited by purine and pyrimidine nucleotides.
5
Wang, Ying-Kai, Sungdae Park, B. Tracy Nixon та Timothy R. Hoover. "Nucleotide-Dependent Conformational Changes in the σ54-Dependent Activator DctD". Journal of Bacteriology 185, № 20 (2003): 6215–19. http://dx.doi.org/10.1128/jb.185.20.6215-6219.2003.
Full textAbstract:
ABSTRACT Activators of σ54-RNA polymerase holoenzyme couple ATP hydrolysis to formation of an open promoter complex. DctDΔ1-142, a truncated and constitutively active form of the σ54-dependent activator DctD from Sinorhizobium meliloti, displayed an altered DNase I footprint at its binding site located upstream of the dctA promoter in the presence of ATP. The altered footprint was not observed for a mutant protein with a substitution at or near the putative arginine finger, a conserved arginine residue thought to contact the nucleotide. These data suggest that structural changes in DctDΔ1-142 during ATP hydrolysis can be detected by alterations in the DNase I footprint of the protein and may be communicated by interactions between bound nucleotide and the arginine finger. In addition, kinetic data for changes in fluorescence energy transfer upon binding of 2′(3′)-O-(N-methylanthraniloyl)-ATP (Mant-ATP) to DctDΔ1-142 and DctD suggested that these proteins undergo multiple conformational changes following ATP binding.
6
Szulc, Aleksandra, Maria Zablocka, Yannick Coppel, et al. "A viologen phosphorus dendritic molecule as a carrier of ATP and Mant-ATP: spectrofluorimetric and NMR studies." New J. Chem. 38, no. 12 (2014): 6212–22. http://dx.doi.org/10.1039/c4nj01176g.
Full text
7
Ghosh, Abhrajyoti, Sophia Hartung, Chris van der Does, John A. Tainer, and Sonja-Verena Albers. "Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding." Biochemical Journal 437, no. 1 (2011): 43–52. http://dx.doi.org/10.1042/bj20110410.
Full textAbstract:
Microbial motility frequently depends on flagella or type IV pili. Using recently developed archaeal genetic tools, archaeal flagella and its assembly machinery have been identified. Archaeal flagella are functionally similar to bacterial flagella and their assembly systems are homologous with type IV pili assembly systems of Gram-negative bacteria. Therefore elucidating their biochemistry may result in insights in both archaea and bacteria. FlaI, a critical cytoplasmic component of the archaeal flagella assembly system in Sulfolobus acidocaldarius, is a member of the type II/IV secretion system ATPase superfamily, and is proposed to be bi-functional in driving flagella assembly and movement. In the present study we show that purified FlaI is a Mn2+-dependent ATPase that binds MANT-ATP [2′-/3′-O-(N′- methylanthraniloyl)adenosine-5′-O-triphosphate] with a high affinity and hydrolyses ATP in a co-operative manner. FlaI has an optimum pH and temperature of 6.5 and 75 °C for ATP hydrolysis. Remarkably, archaeal, but not bacterial, lipids stimulated the ATPase activity of FlaI 3–4-fold. Analytical gel filtration indicated that FlaI undergoes nucleotide-dependent oligomerization. Furthermore, SAXS (small-angle X-ray scattering) analysis revealed an ATP-dependent hexamerization of FlaI in solution. The results of the present study report the first detailed biochemical analyses of the motor protein of an archaeal flagellum.
8
Chaudhury, Paushali, Chris van der Does, and Sonja-Verena Albers. "Characterization of the ATPase FlaI of the motor complex of the Pyrococcus furiosus archaellum and its interactions between the ATP-binding protein FlaH." PeerJ 6 (June 18, 2018): e4984. http://dx.doi.org/10.7717/peerj.4984.
Full textAbstract:
The archaellum, the rotating motility structure of archaea, is best studied in the crenarchaeon Sulfolobus acidocaldarius. To better understand how assembly and rotation of this structure is driven, two ATP-binding proteins, FlaI and FlaH of the motor complex of the archaellum of the euryarchaeon Pyrococcus furiosus, were overexpressed, purified and studied. Contrary to the FlaI ATPase of S. acidocaldarius, which only forms a hexamer after binding of nucleotides, FlaI of P. furiosus formed a hexamer in a nucleotide independent manner. In this hexamer only 2 of the ATP binding sites were available for binding of the fluorescent ATP-analog MANT-ATP, suggesting a twofold symmetry in the hexamer. P. furiosus FlaI showed a 250-fold higher ATPase activity than S. acidocaldarius FlaI. Interaction studies between the isolated N- and C-terminal domains of FlaI showed interactions between the N- and C-terminal domains and strong interactions between the N-terminal domains not previously observed for ATPases involved in archaellum assembly. These interactions played a role in oligomerization and activity, suggesting a conformational state of the hexamer not observed before. Further interaction studies show that the C-terminal domain of PfFlaI interacts with the nucleotide binding protein FlaH. This interaction stimulates the ATPase activity of FlaI optimally at a 1:1 stoichiometry, suggesting that hexameric PfFlaI interacts with hexameric PfFlaH. These data help to further understand the complex interactions that are required to energize the archaellar motor.
9
Yu, Yadong, Haichuan Liu, Zanlin Yu, H. Ewa Witkowska, and Yifan Cheng. "Stoichiometry of Nucleotide Binding to Proteasome AAA+ ATPase Hexamer Established by Native Mass Spectrometry." Molecular & Cellular Proteomics 19, no. 12 (2020): 1997–2014. http://dx.doi.org/10.1074/mcp.ra120.002067.
Full textAbstract:
AAA+ ATPases constitute a large family of proteins that are involved in a plethora of cellular processes including DNA disassembly, protein degradation and protein complex disassembly. They typically form a hexametric ring-shaped structure with six subunits in a (pseudo) 6-fold symmetry. In a subset of AAA+ ATPases that facilitate protein unfolding and degradation, six subunits cooperate to translocate protein substrates through a central pore in the ring. The number and type of nucleotides in an AAA+ ATPase hexamer is inherently linked to the mechanism that underlies cooperation among subunits and couples ATP hydrolysis with substrate translocation. We conducted a native MS study of a monodispersed form of PAN, an archaeal proteasome AAA+ ATPase, to determine the number of nucleotides bound to each hexamer of the WT protein. We utilized ADP and its analogs (TNP-ADP and mant-ADP), and a nonhydrolyzable ATP analog (AMP-PNP) to study nucleotide site occupancy within the PAN hexamer in ADP- and ATP-binding states, respectively. Throughout all experiments we used a Walker A mutant (PANK217A) that is impaired in nucleotide binding as an internal standard to mitigate the effects of residual solvation on mass measurement accuracy and to serve as a reference protein to control for nonspecific nucleotide binding. This approach led to the unambiguous finding that a WT PAN hexamer carried – from expression host – six tightly bound ADP molecules that could be exchanged for ADP and ATP analogs. Although the Walker A mutant did not bind ADP analogs, it did bind AMP-PNP, albeit at multiple stoichiometries. We observed variable levels of hexamer dissociation and an appearance of multimeric species with the over-charged molecular ion distributions across repeated experiments. We posit that these phenomena originated during ESI process at the final stages of ESI droplet evolution.
10
Lin, Bin, Kelly L. Covalle, and Janine R. Maddock. "The Caulobacter crescentus CgtA Protein Displays Unusual Guanine Nucleotide Binding and Exchange Properties." Journal of Bacteriology 181, no. 18 (1999): 5825–32. http://dx.doi.org/10.1128/jb.181.18.5825-5832.1999.
Full textAbstract:
ABSTRACT The Caulobacter crescentus CgtA protein is a member of the Obg-GTP1 subfamily of monomeric GTP-binding proteins. In vitro, CgtA specifically bound GTP and GDP but not GMP or ATP. CgtA bound GTP and GDP with moderate affinity at 30°C and displayed equilibrium binding constants of 1.2 and 0.5 μM, respectively, in the presence of Mg2+. In the absence of Mg2+, the affinity of CgtA for GTP and GDP was reduced 59- and 6-fold, respectively.N-Methyl-3′-O-anthranoyl (mant)–guanine nucleotide analogs were used to quantify GDP and GTP exchange. Spontaneous dissociation of both GDP and GTP in the presence of 5 to 12 mM Mg2+ was extremely rapid (kd = 1.4 and 1.5 s−1, respectively), 103- to 105-fold faster than that of the well-characterized eukaryotic Ras-like GTP-binding proteins. The dissociation rate constant of GDP increased sevenfold in the absence of Mg2+. Finally, there was a low inherent GTPase activity with a single-turnover rate constant of 5.0 × 10−4s−1 corresponding to a half-life of hydrolysis of 23 min. These data clearly demonstrate that the guanine nucleotide binding and exchange properties of CgtA are different from those of the well-characterized Ras-like GTP-binding proteins. Furthermore, these data are consistent with a model whereby the nucleotide occupancy of CgtA is controlled by the intracellular levels of guanine nucleotides.
Dissertations / Theses on the topic "Mant-ATP"
1
Feofilova, Maria. "Probing Dynein Motor Activity in the Intact Chlamydomonas Axoneme." 2017. https://tud.qucosa.de/id/qucosa%3A34182.
Full textAbstract:
Eukaryotic flagella and cilia are long rod-like extensions of cells, which play a fundamental role in single cell movement, as well as in fluid transport. Flagella and cilia contain a highly evolutionary conserved mechanical structure called the axoneme. The motion of the flagellum is generated by dynein motor proteins, located all along the length of the axonemal structure.
Fluorescent ATP analogs have been a useful tool to study ATPase activity of various motor proteins. \acrfull{mant} has been previously used to probe the activity of various ATPases, including dynein. It has been shown by various authors, that MANT-ATP supports dynein activity as well as the axonemal beat. However, direct observations of binding to the axonemal structure were not previously reported.
Using highly sensitive fluorescent microscopy to monitor the binding of the fluorescent ATP analog, I probed dynein activity directly in the immobilized intact axoneme for the first time.
To understand these kinetics a kinetic model was developed. By fitting this model to experimental data I was able to identify ATP-binding sites with distinct kinetic properties in the axoneme.
I report a turnover rate of k = 0.02 s−1 at 1μM mant-ATP for dynein. Moreover, I discovered that there is binding of the ATP analog to the axoneme with a much higher rate of k = 11 s−1 at 1μM mant-ATP. By the application of this method to axonemes with reduced dyneins, it has been identified that the slow rate belongs to dynein.