Fungal AreA is a key nitrogen metabolism transcription factor in nitrogen metabolism repression (NMR). Studies have shown that there are different ways to regulate AreA activity in yeast and filamentous ascomycetes, but in Basidiomycota, how AreA is regulated is unknown. Here, a gene from Ganoderma lucidum with similarity to nmrA of filamentous ascomycetes was identified. The NmrA interacted with the C-terminal of AreA according to yeast two-hybrid assay. In order to determine the effect of NmrA...
[NMR paper] Chemical shifts-based similarity restraints improve accuracy of RNA structures determined via NMR.
Chemical shifts-based similarity restraints improve accuracy of RNA structures determined via NMR.
Chemical shifts-based similarity restraints improve accuracy of RNA structures determined via NMR.
RNA. 2020 Sep 11;:
Authors: Lawrence C, Grishaev AV
Abstract
Determination of structure of RNA via NMR is complicated in large part by the lack of a precise parameterization linking the observed chemical shifts to the underlying geometric parameters. In contrast to proteins, where numerous high-resolution crystal structures serve as...
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09-15-2020 04:44 AM
[NMR paper] Functional Analysis of the Nitrogen Metabolite Repression Regulator Gene nmrA in Aspergillus flavus.
Functional Analysis of the Nitrogen Metabolite Repression Regulator Gene nmrA in Aspergillus flavus.
Related Articles Functional Analysis of the Nitrogen Metabolite Repression Regulator Gene nmrA in Aspergillus flavus.
Front Microbiol. 2016;7:1794
Authors: Han X, Qiu M, Wang B, Yin WB, Nie X, Qin Q, Ren S, Yang K, Zhang F, Zhuang Z, Wang S
Abstract
In Aspergillus nidulans, the nitrogen metabolite repression (NMR) regulator NmrA plays a major role in regulating the activity of the GATA transcription factor AreA during nitrogen...
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12-11-2016 06:23 AM
[NMR paper] NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.
NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.
Related Articles NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.
J Mol Biol. 2014 May 13;
Authors: Serrano P, Geralt M, Mohanty B, Wüthrich K
Abstract
NMR structures of ?-subunits, which are recently discovered ?-proteobacterial F1F0-ATPase regulatory proteins representing a Pfam protein family of 246 sequences from 219 species (PF07345), exhibit a four-helix bundle, which is different from all other known F1F0-ATPase inhibitors. Chemical shift...
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05-20-2014 11:10 PM
[NMR paper] Identification of fragments targeting an alternative pocket on HIV-1 gp41 by NMR screening and similarity searching.
Identification of fragments targeting an alternative pocket on HIV-1 gp41 by NMR screening and similarity searching.
Identification of fragments targeting an alternative pocket on HIV-1 gp41 by NMR screening and similarity searching.
Bioorg Med Chem Lett. 2013 Jul 22;
Authors: Chu S, Gochin M
Abstract
The HIV-1 envelope glycoprotein gp41 fusion intermediate is a promising drug target for inhibiting viral entry. However, drug development has been impeded by challenges inherent in mediating the underlying protein-protein interaction. Here...
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Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Eur Biophys J. 2011 Apr 7;
Authors: Cukier CD, Ramos A
Here we review the role played by transient interactions between multi-functional proteins and their RNA targets in the regulation of mRNA metabolism, and we describe the important function of NMR spectroscopy in the study of these systems. We place emphasis on a general approach for the study of different features of modular multi-domain...
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[NMR paper] NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans
NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
Related Articles NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
J Mol Biol. 2000 Aug 25;301(4):1003-17
Authors: Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P
The 131-amino acid residue...
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11-19-2010 08:29 PM
[NMR paper] 1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorp
1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
Related Articles 1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
Proteins. 1998 Aug 15;32(3):334-49
Authors: Bloch C, Patel SU, Baud F, Zvelebil MJ, Carr MD, Sadler PJ, Thornton JM
The three-dimensional structure of the Sorghum bicolor seed protein gamma-thionin SIalpha1 has been determined by 2D 1H nuclear magnetic resonance (NMR) spectroscopy. The secondary structure of this 47-residue antifungal...
A Gene from Ganoderma lucidum with Similarity to nmrA of Filamentous Ascomycetes Contributes to Regulating AreA
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