Comparison of base inclination in ribo‐AU and deoxyribo‐AT polymers

Jin, Xiaokui; Johnson, W. Curtis

doi:10.1002/bip.360360305

Cited by 3 publications

(1 citation statement)

References 46 publications

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“…However, it is important to note that the presence of deoxyribonucleotides did not affect the spectroscopic signals either of both fluorescence and far-UV CD, because DNA is spectroscopically silent in fluorescence, and in the far-UV region of CD spectra between 210–240 nm, deoxyribonucleotides do not absorb [ 44 , 45 ]. It is also interesting to note that deoxyoligonucleotides in aqueous solution or intact DNA show a small or slightly positive ellipticity around 222 nm [ 45 , 46 , 47 , 48 , 49 ] where we have carried out the study of the CD biophysical properties of the protein (see Results section).…”

Section: Methodsmentioning

confidence: 99%

The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties

Contreras

Sevilla

Cámara-Artigas

et al. 2018

IJMS

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The LrtA protein of Synechocystis sp. PCC 6803 intervenes in cyanobacterial post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family of proteins, involved in protein synthesis. In this work, we studied the conformational preferences and stability of isolated LrtA in solution. At physiological conditions, as shown by hydrodynamic techniques, LrtA was involved in a self-association equilibrium. As indicated by Nuclear Magnetic Resonance (NMR), circular dichroism (CD) and fluorescence, the protein acquired a folded, native-like conformation between pH 6.0 and 9.0. However, that conformation was not very stable, as suggested by thermal and chemical denaturations followed by CD and fluorescence. Theoretical studies of its highly-charged sequence suggest that LrtA had a Janus sequence, with a context-dependent fold. Our modelling and molecular dynamics (MD) simulations indicate that the protein adopted the same fold observed in other members of the HPF family (β-α-β-β-β-α) at its N-terminal region (residues 1–100), whereas the C terminus (residues 100–197) appeared disordered and collapsed, supporting the overall percentage of overall secondary structure obtained by CD deconvolution. Then, LrtA has a chameleonic sequence and it is the first member of the HPF family involved in a self-association equilibrium, when isolated in solution.

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Section: Methodsmentioning

confidence: 99%

The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties

Contreras

Sevilla

Cámara-Artigas

et al. 2018

IJMS

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Clinical analysis of 12 patients with primary lymphoepithelial carcinoma of the parotid gland

Deng

Zhou

et al. 2021

Eur Arch Otorhinolaryngol

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The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue

Neira

Lopez

Sevilla

et al. 2018

Biochemical Journal

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NUPR1 is a protumoral multifunctional intrinsically disordered protein (IDP), which is activated during the acute phases of pancreatitis. It interacts with other IDPs such as prothymosin α, as well as with folded proteins such as the C-terminal region of RING1-B (C-RING1B) of the Polycomb complex; in all those interactions, residues around Ala33 and Thr68 (the 'hot-spot' region) of NUPR1 intervene. Its paralogue, NUPR1L, is also expressed in response to DNA damage, it is p53-regulated, and its expression down-regulates that of the gene. In this work, we characterized the conformational preferences of isolated NUPR1L and its possible interactions with the same molecular partners of NUPR1. Our results show that NUPR1L was an oligomeric IDP from pH 2.0 to 12.0, as judged by steady-state fluorescence, circular dichroism (CD), dynamic light scattering, 1DH-NMR (nuclear magnetic resonance), and as indicated by structural modelling. However, in contrast with NUPR1, there was evidence of local helical- or turn-like structures; these structures were not rigid, as judged by the lack of sigmoidal behaviour in the chemical and thermal denaturation curves obtained by CD and fluorescence. Interestingly enough, NUPR1L interacted with prothymosin α and C-RING1B, and with a similar affinity to that of NUPR1 (in the low micromolar range). Moreover, NUPR1L hetero-associated with NUPR1 with an affinity of 0.4 µM and interacted with the 'hot-spot' region of NUPR1. Thus, we suggest that the regulation of gene by NUPR1L does not only happen at the DNA level, but it could also involve direct interactions with NUPR1 natural partners.

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Comparison of base inclination in ribo‐AU and deoxyribo‐AT polymers

Cited by 3 publications

References 46 publications

The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties

The Cyanobacterial Ribosomal-Associated Protein LrtA from Synechocystis sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties

Clinical analysis of 12 patients with primary lymphoepithelial carcinoma of the parotid gland

The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue

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