Influence of simple polypeptides on nucleotide polymerization

1986 ◽  
Vol 16 (3-4) ◽  
pp. 452-453
Author(s):  
Bernard Barbier ◽  
André Brack
Keyword(s):  
Nucleotide Polymerization

scholarly journals Structural basis of reverse nucleotide polymerization

2013 ◽  
Vol 110 (52) ◽  
pp. 20970-20975 ◽  
Author(s):  
A. Nakamura ◽  
T. Nemoto ◽  
I. U. Heinemann ◽  
K. Yamashita ◽  
T. Sonoda ◽  
...  
Keyword(s):  
Structural Basis ◽  
Nucleotide Polymerization

Dual-color control of nucleotide polymerization sensed by a fluorescence actuator

2014 ◽  
Vol 13 (5) ◽  
pp. 751-756 ◽  
Author(s):  
Madalena M. Reimão-Pinto ◽  
Ana Cordeiro ◽  
Carina Almeida ◽  
André V. Pinheiro ◽  
Artur Moro ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Temporal Control ◽  
Dual Color ◽  
Color Control ◽  
Nucleotide Polymerization

Spatial and temporal control of molecular mechanisms can be achieved using photolabile bonds that connect biomolecules to protective caging groups, which can be cleaved upon irradiation of a specific wavelength, releasing the biomolecule ready-to-use.

The catalysis of nucleotide polymerization by compounds of divalent lead

1979 ◽  
Vol 12 (4) ◽  
pp. 357-364 ◽  
Author(s):  
H. L. Sleeper ◽  
L. E. Orgel
Keyword(s):  
Nucleotide Polymerization

scholarly journals Mechanism for priming DNA synthesis by yeast DNA Polymerase α

eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
Rajika L Perera ◽  
Rubben Torella ◽  
Sebastian Klinge ◽  
Mairi L Kilkenny ◽  
Joseph D Maman ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Catalytic Core ◽  
Dna Polymerase Α ◽  
Dna Oligonucleotides ◽  
Computational Data ◽  
Dna Template ◽  
Lagging Strand ◽  
Primase Complex ◽  
Nucleotide Polymerization

The DNA Polymerase α (Pol α)/primase complex initiates DNA synthesis in eukaryotic replication. In the complex, Pol α and primase cooperate in the production of RNA-DNA oligonucleotides that prime synthesis of new DNA. Here we report crystal structures of the catalytic core of yeast Pol α in unliganded form, bound to an RNA primer/DNA template and extending an RNA primer with deoxynucleotides. We combine the structural analysis with biochemical and computational data to demonstrate that Pol α specifically recognizes the A-form RNA/DNA helix and that the ensuing synthesis of B-form DNA terminates primer synthesis. The spontaneous release of the completed RNA-DNA primer by the Pol α/primase complex simplifies current models of primer transfer to leading- and lagging strand polymerases. The proposed mechanism of nucleotide polymerization by Pol α might contribute to genomic stability by limiting the amount of inaccurate DNA to be corrected at the start of each Okazaki fragment.

scholarly journals Piece of the Puzzle: Remdesivir disassemble the multimeric SARS-CoV-2 RNA-dependent RNA Polymerase Non-Structural Proteins (RdRp-NSPs) complex

2020 ◽  
Author(s):  
Fisayo A. Olotu ◽  
Kehinde F. Omolabi ◽  
Mahmoud E. S Soliman
Keyword(s):  
Rna Polymerase ◽  
Rna Replication ◽  
Mortality Rates ◽  
Viral Rna ◽  
Residue Pair ◽  
Structural Proteins ◽  
Rna Dependent Rna Polymerase ◽  
Replication Process ◽  
First Time ◽  
Nucleotide Polymerization

Abstract The recently emerged SARS-like coronavirus (SARS-CoV-2) has continued to spread rapidly among humans with alarming upsurges in global mortality rates. A major key to tackling this virus is to disrupt its RNA replication process as previously reported for Remdesivir (Rem-P3). For the first time, we modeled the binding of Rem-P3 to SARS-CoV-2 RdRp-NSPs complex, a multimeric assembly that drives viral RNA replication in human hosts. Findings revealed that while ATP-binding stabilized the replicative tripartite, Rem-P3 disintegrated the RdRp-NSP complex, starting with the detachment of the NSP7-NSP8 heterodimer followed by minimal displacement of the second NSP8 subunit (NSP8II). More so, Rem-P3 interacted with a relatively higher affinity (ΔGbind) while inducing high perturbations across the RdRp-NSP domains. D452, T556, V557, S682, and D760 were identified for their crucial roles in stacking the cyano-adenosine and 3,4-dihydroxyoxolan rings of Rem-P3 while its flexible P3 tail extended towards the palm domain blocking D618 and K798; a residue-pair identified for essential roles in RNA replication. However, ATP folded away from D618 indicative of a more coordinated binding favorable for nucleotide polymerization. We believe findings from this study will significantly contribute to the structure-based design of novel disruptors of the SARS-CoV-2 RNA replicative machinery.

ACTION OF KI AND SEVERAL IODOCOMPOUNDS ON [3H]URIDINE INCORPORATION INTO THYROID RNA

1978 ◽  
Vol 89 (2) ◽  
pp. 316-322 ◽  
Author(s):  
D. L. Kleiman de Pisarev ◽  
M. A. Pisarev ◽  
G. J. Juvenal
Keyword(s):  
Paper Chromatography ◽  
Cyclic Nucleotide ◽  
Inhibitory Action ◽  
Distribution Space ◽  
Uridine Incorporation ◽  
Uridine Uptake ◽  
Molar Basis ◽  
Camp And Cgmp ◽  
Nucleotide Polymerization

ABSTRACT The present studies were performed in order to further clarify the action of iodine and iodocompounds on the incorporation of labelled uridine into thyroid RNA. KI decreased RNA labelling but did not alter total [3H] uridine uptake or [3H]inulin distribution space. KI also inhibited the increase in RNA labelling produced by 8 mm glucose. T4 was more potent on a molar basis than KI in impairing uridine incorporation. TETRAC, TRIAC and isopropyl-T3 also decreased RNA labelling, while T2 and isopropyl-T2 were ineffective. KI did not alter the distribution of the uridine derivatives, UMP, UDP and UTP, as determined by the distribution of [3H] uridine in these compounds by paper chromatography, suggesting that the action of KI does not take place at the step of uridine phosphorylation. Like its effect on TSH, KI also impairs the stimulatory effect of exogenous cAMP and cGMP on RNA labelling, suggesting that its action is exerted beyond the step of cyclic nucleotide formation. Iodine and iodocompounds may exert their inhibitory action on RNA labelling at the step of nucleotide polymerization.

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