2'-deoxyadenosine-5'-phosphate/5'-Adenylic acid, 2'-deoxy-/5'-Adenylic acid, 2'-deoxy- (9CI)/9-(2-Deoxy-5-O-phosphono-β-D-erythro-pentofuranosyl)-9H-purin-6-amin/2'-Deoxy-5'-AMP/2'-Deoxy-5'-adenylate/2'-Deoxyadenosine 5'-monophosphate/2'-Deoxyadenylate/Adenosine, 2'-deoxy-, 5'-(dihydrogen phosphate) (8CI)/Adenosine, 2'-deoxy-, 5'-(dihydrogen phosphate) (6CI,8CI)/Deoxyadenosine monophosphate/2'-Deoxyadenosine-5'-monophosphoric acid/2'-deoxy-5'-adenosine monophosphate/2'-Deoxyadenosine 5'-phosphate/deoxyadenosine 5'-monophosphate/d-AMP/dAMP/deoxyadenosine 5'-phosphate/[(2R,3S,5R)-5-(6-Amino-9H-purin-9-yl)-3-hydroxytetrahydro-2-furanyl]methyl dihydrogen phosphate/2'-deoxy-Adenosine 5'-phosphorate/Deoxy-5'-adenylate/2'-deoxyadenosine monophosphate/2'-Deoxyadenosine-5'-monophosphate
[(2R,3S,5R)-5-(6-aminopurin-9-yl)-3-hydroxyoxolan-2-yl]methyl dihydrogen phosphate
753.5±70.0 °C at 760 mmHg
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provides coniferyl ferulate(CAS#:653-63-4) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
ADP-ribosylation refers to the addition of one or more ADP-ribose groups onto proteins. The attached ADP-ribose monomers or polymers, commonly known as poly(ADP-ribose) (PAR), modulate the activities of the modified substrates or their binding affinities to other proteins. However, progress in this area is hindered by a lack of tools to investigate this protein modification. Here, we describe a new method named ELTA (enzymatic labeling of terminal ADP-ribose) for labeling free or protein-conjugated ADP-ribose monomers and polymers at their 2′-OH termini using the enzyme OAS1 and dATP. When coupled with various dATP analogs (e.g., radioactive, fluorescent, affinity tags), ELTA can be used to explore PAR biology with techniques routinely used to investigate DNA or RNA function. We demonstrate that ELTA enables the biophysical measurements of protein binding to PAR of a defined length, detection of PAR length from proteins and cells, and enrichment of sub-femtomole amounts of ADP-ribosylated peptides from cell lysates.
ADP-ribose; ADP-ribosylated protein; ADP-ribosylation; ADP-ribosyltransferase; enzymatic labeling; mono(ADP-ribosyl)ated protein; oligoadenylate synthetase; poly(ADP-ribose); poly(ADP-ribose) polymerase; poly(ADP-ribosyl)ated protein.
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando 1, Elad Elkayam 2, Robert Lyle McPherson 1, Morgan Dasovich 1, Shang-Jung Cheng 1, Jim Voorneveld 3, Dmitri V Filippov 3, Shao-En Ong 4, Leemor Joshua-Tor 2, Anthony K L Leung 5
2019 Feb 21;
Solid-state nanopores promise a scalable platform for single-molecule DNA analysis. Direct, real-time identification of nucleobases in DNA strands is still limited by the sensitivity and the spatial resolution of established ionic sensing strategies. Here, we study a different but promising strategy based on optical spectroscopy. We use an optically engineered elongated nanopore structure, a plasmonic nanoslit, to locally enable single-molecule surface enhanced Raman spectroscopy (SERS). Combining SERS with nanopore fluidics facilitates both the electrokinetic capture of DNA analytes and their local identification through direct Raman spectroscopic fingerprinting of four nucleobases. By studying the stochastic fluctuation process of DNA analytes that are temporarily adsorbed inside the pores, we have observed asynchronous spectroscopic behavior of different nucleobases, both individual and incorporated in DNA strands. These results provide evidences for the single-molecule sensitivity and the sub-nanometer spatial resolution of plasmonic nanoslit SERS.
High Spatial Resolution Nanoslit SERS for Single-Molecule Nucleobase Sensing
2018 Apr 30;
The high fidelity of DNA replication and repair is attributable, in part, to the allosteric regulation of ribonucleotide reductases (RNRs) that maintains proper deoxynucleotide pool sizes and ratios in vivo. In class Ia RNRs, ATP (stimulatory) and dATP (inhibitory) regulate activity by binding to the ATP-cone domain at the N terminus of the large α subunit and altering the enzyme’s quaternary structure. Class Ib RNRs, in contrast, have a partial cone domain and have generally been found to be insensitive to dATP inhibition. An exception is the Bacillus subtilis Ib RNR, which we recently reported to be inhibited by physiological concentrations of dATP. Here, we demonstrate that the α subunit of this RNR contains tightly bound deoxyadenosine 5′-monophosphate (dAMP) in its N-terminal domain and that dATP inhibition of CDP reduction is enhanced by its presence. X-ray crystallography reveals a previously unobserved (noncanonical) α2 dimer with its entire interface composed of the partial N-terminal cone domains, each binding a dAMP molecule. Using small-angle X-ray scattering (SAXS), we show that this noncanonical α2 dimer is the predominant form of the dAMP-bound α in solution and further show that addition of dATP leads to the formation of larger oligomers. Based on this information, we propose a model to describe the mechanism by which the noncanonical α2 inhibits the activity of the B. subtilis Ib RNR in a dATP- and dAMP-dependent manner.
ATP-cone; allostery; dAMP; nucleotide metabolism; ribonucleotide reductase.
An Endogenous dAMP Ligand in Bacillus subtilis Class Ib RNR Promotes Assembly of a Noncanonical Dimer for Regulation by dATP
Mackenzie J Parker 1, Ailiena O Maggiolo 2, William C Thomas 3, Albert Kim 1, Steve P Meisburger 3, Nozomi Ando 4, Amie K Boal 5 6, JoAnne Stubbe 7 8
2018 May 15;