Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy

2015 ◽  
Vol 14 (2) ◽  
pp. 252-257 ◽  
Author(s):  
Monika Heilmann ◽  
John M. Christie ◽  
John T. M. Kennis ◽  
Gareth I. Jenkins ◽  
Tilo Mathes
Keyword(s):  
Fluorescence Spectroscopy ◽  
Quantum Efficiency ◽  
Structural Transformations ◽  
Side Chains ◽  
Molecular Signaling ◽  
Signaling Mechanism ◽  
Photoinduced Transformation ◽  
Tryptophan Side Chains

The plant photoreceptor UVR8 uses tryptophan side chains to absorb UV-B radiation to induce photoprotective responses via a so far unknown molecular signaling mechanism. We investigated structural transformations and quantum efficiency of UVR8 photoactivation by vibrational and fluorescence spectroscopy.

Calculated Raman Optical Activity Signatures of Tryptophan Side Chains

ChemPhysChem ◽  
2008 ◽  
Vol 9 (15) ◽  
pp. 2177-2180 ◽  
Author(s):  
Christoph R. Jacob ◽  
Sandra Luber ◽  
Markus Reiher
Keyword(s):  
Optical Activity ◽  
Side Chains ◽  
Raman Optical Activity ◽  
Tryptophan Side Chains

HCN, A Triple-Resonance NMR Technique for Selective Observation of Histidine and Tryptophan Side Chains in13C/15N-Labeled Proteins

1996 ◽  
Vol 113 (3) ◽  
pp. 236-247 ◽  
Author(s):  
James L. Sudmeier ◽  
Elissa L. Ash ◽  
Ulrich L. Günther ◽  
Xuelian Luo ◽  
Peter A. Bullock ◽  
...  
Keyword(s):  
Side Chains ◽  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Tryptophan Side Chains

scholarly journals Localising individual atoms of tryptophan side chains in the metallo-<i>β</i>-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites

2022 ◽  
Vol 3 (1) ◽  
pp. 1-13
Author(s):  
Henry W. Orton ◽  
Iresha D. Herath ◽  
Ansis Maleckis ◽  
Shereen Jabar ◽  
Monika Szabo ◽  
...  
Keyword(s):  
Active Site ◽  
Side Chains ◽  
Pseudocontact Shifts ◽  
Magnetic Susceptibility Anisotropy ◽  
Single Crystal Structures ◽  
Flexible Loop ◽  
Backbone Amide ◽  
Tryptophan Residues ◽  
Atomic Coordinates ◽  
Tryptophan Side Chains

Abstract. The metallo-β-lactamase IMP-1 features a flexible loop near the active site that assumes different conformations in single crystal structures, which may assist in substrate binding and enzymatic activity. To probe the position of this loop, we labelled the tryptophan residues of IMP-1 with 7-13C-indole and the protein with lanthanoid tags at three different sites. The magnetic susceptibility anisotropy (Δχ) tensors were determined by measuring pseudocontact shifts (PCSs) of backbone amide protons. The Δχ tensors were subsequently used to identify the atomic coordinates of the tryptophan side chains in the protein. The PCSs were sufficient to determine the location of Trp28, which is in the active site loop targeted by our experiments, with high accuracy. Its average atomic coordinates showed barely significant changes in response to the inhibitor captopril. It was found that localisation spaces could be defined with better accuracy by including only the PCSs of a single paramagnetic lanthanoid ion for each tag and tagging site. The effect was attributed to the shallow angle with which PCS isosurfaces tend to intersect if generated by tags and tagging sites that are identical except for the paramagnetic lanthanoid ion.

scholarly journals Pigment Epithelium-Derived Factor and its Phosphomimetic Mutant Induce JNK-Dependent Apoptosis and P38-Mediated Migration Arrest

2018 ◽  
Vol 49 (2) ◽  
pp. 512-529 ◽  
Author(s):  
Alexander Konson ◽  
Sunila Pradeep ◽  
Cosimo Walter D’Acunto ◽  
Rony Seger
Keyword(s):  
Cancer Cells ◽  
Present Report ◽  
Pigment Epithelium ◽  
Cellular Level ◽  
Molecular Signaling ◽  
Antiangiogenic Effect ◽  
Signaling Mechanism ◽  
Pigment Epithelium Derived Factor ◽  
And Migration

Background/Aims: Pigment epithelium-derived factor (PEDF) is a potent endogenous inhibitor of angiogenesis, and a promising anticancer agent. We have previously shown that PEDF can be phosphorylated, and that distinct phosphorylations differentially regulate its physiological functions. We also demonstrated that triple phosphomimetic mutant (EEE-PEDF), has significantly increased antiangiogenic activity, and is much more efficient than WT-PEDF in inhibiting neovascularization and tumor growth. The enhanced antiangiogenic effect was associated with a direct ability to facilitate apoptosis of tumor-residing endothelial cells (EC), and subsequently, disruption of intratumoral vascularization. In the present report, we elucidated the molecular mechanism by which EEE-PEDF exerts more profound effects at the cellular level. Methods: Here we used Western blotting, as well as in vitro binding, proliferation, apoptosis and migration assays to follow the signaling components responsible for the PEDF and EEE-PEDF effects. Results: We found that EEE-PEDF suppresses EC proliferation due to caspase-3-dependent apoptosis, and also inhibits migration of the EC much better than WT-PEDF. Although WT-PEDF and EEE-PEDF did not affect proliferation and did not induce apoptosis of cancer cells, these agents efficiently inhibited cancer cell motility, with EEE-PEDF showing stronger effect. The stronger activity of EEE-PEDF was correlated to a better binding to laminin receptors. Furthermore, the proapoptotic and antimigratory activities of WT-PEDF and EEE-PEDF were found respectively regulated by differential activation of two distinct MAPK pathways, namely JNK and p38. We show that JNK and p38 phosphorylation is much higher in cells treated with EEE-PEDF. JNK leads to apoptosis of ECs, while p38 leads to antimigratory effect in both EC and cancer cells. Conclusion: These results reveal the molecular signaling mechanism by which the phosphorylated PEDF exerts its stronger antiangiogenic, antitumor activities.

A Cost-Effective Labeling Strategy for the NMR Study of Large Proteins: Selective15N-Labeling of the Tryptophan Side Chains of Prolyl Oligopeptidase

ChemBioChem ◽  
2009 ◽  
Vol 10 (17) ◽  
pp. 2736-2739 ◽  
Author(s):  
Teresa Tarragó ◽  
Birgit Claasen ◽  
Nessim Kichik ◽  
Ricard A. Rodriguez-Mias ◽  
Margarida Gairí ◽  
...  
Keyword(s):  
Cost Effective ◽  
Side Chains ◽  
Prolyl Oligopeptidase ◽  
Large Proteins ◽  
Nmr Study ◽  
Tryptophan Side Chains
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