4.4 Article

The dityrosine cross-link as an intrinsic donor for assembling FRET pairs in the study of protein structure

Journal

BIOPHYSICAL CHEMISTRY
Volume 170, Issue -, Pages 1-8

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2012.07.001

Keywords

Conformational change; Dityrosine; FRET; Galleria mellonella; JHBP

Funding

  1. Polish Ministry of Science and Higher Education [018/B/P01/2009/37]

Ask authors/readers for more resources

Dityrosine-Lucifer yellow (DT-LY) was used as the donor-acceptor pair in studies of the topography of juvenile hormone-binding protein (JHBP). The Forster distance, R-0 = 30.5 angstrom for DT-LY was determined. Separation distances (R) between DT and the fluorescent probes placed at the 219 and 224 position were 26 and 28 angstrom and correspond to that found from X-ray analysis (23 and 24 angstrom, respectively). Higher than expected efficiency of energy transfer between DT and LY probe placed in position 171 was observed, indicating that this probe is immobilized in the protein structure (kappa(2) = 3.25). Red-edge excitation shift (REES) analysis supported this assumption. Slight changes in Forster resonance energy transfer (FRET) efficiency were observed after incubating the labeled proteins with juvenile hormone III (JH III). This is the first report showing the application of DT fluorescence for the analysis of protein conformation. (c) 2012 Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

Article Biochemistry & Molecular Biology

Destabilisation of the structure of transthyretin is driven by Ca2+

Elzbieta Wieczorek, Sylwia Kedracka-Krok, Dominika Bystranowska, Maciej Ptak, Karolina Wiak, Zofia Wygralak, Urszula Jankowska, Andrzej Ozyhar

Summary: This study found that Ca2+ does not induce TTR dissociation or oligomerization, but does alter the conformational flexibility of TTR and its interactions with solvent molecules, leading to the formation of non-native TTR conformers and destabilization of TTR structure.

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES (2021)

Article Biochemistry & Molecular Biology

Natural Mutations Affect Structure and Function of gC1q Domain of Otolin-1

Rafal Holubowicz, Andrzej Ozyhar, Piotr Dobryszycki

Summary: This study demonstrates how natural variants in the gC1q domain of otolin-1 affect protein stability and calcium binding ability, and how these mutations can impact the function of otolin-1.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)

Review Biochemistry & Molecular Biology

The Multifaceted Nature of Nucleobindin-2 in Carcinogenesis

Anna Skorupska, Rafal Lenda, Andrzej Ozyhar, Dominika Bystranowska

Summary: Nucb2 is a multifunctional protein involved in various biological processes, including carcinogenesis. Studies have shown that Nucb2 and its derivative nesfatin-1 play a dual role in tumorigenesis, with both pro-metastatic and anti-metastatic effects depending on the tissue. The multifaceted nature of Nucb2/nesfatin-1 in carcinogenesis and the apoptosis process is highlighted.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)

Article Multidisciplinary Sciences

Molecular mechanism of calcium induced trimerization of C1q-like domain of otolin-1 from human and zebrafish

Rafal Holubowicz, Andrzej Ozyhar, Piotr Dobryszycki

Summary: The study revealed that the structural stability of zebrafish gC1q domain was lower than the human counterpart under all conditions and required higher concentrations of Ca2+ for stabilization. In contrast, the human gC1q otolin-1 seemed to be optimized to function efficiently at lower concentrations of Ca2+, consistent with reported Ca2+ levels in the endolymph of fish and mammals.

SCIENTIFIC REPORTS (2021)

Review Cell Biology

Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases

Elzbieta Wieczorek, Andrzej Ozyhar

Summary: TTR plays multiple roles in the body, serving as an indicator of nutrition status and a neuroprotective factor. The structural stability of TTR is closely linked to oxidative stress and Ca2+, which may contribute to the development of TTR-related diseases.

CELLS (2021)

Article Chemistry, Multidisciplinary

Controlling the conformational stability of coiled-coil peptides with a single stereogenic center of a peripheral β-amino acid residue

Monika Szefczyk, Katarzyna Ozga, Magda Drewniak-Switalska, Ewa Rudzinska-Szostak, Rafal Holubowicz, Andrzej Ozyhar, Lukasz Berlicki

Summary: The relationship between monomer structure and conformational properties at the oligomer level in foldamers remains a key issue in research. This study focused on the folding of peptidomimetic foldamers and factors affecting their conformational stability, specifically exploring the impact of peptide peripheral modification with trans- and cis-2-aminocyclopentanecarboxylic acid (ACPC) on the structure and stability of a model coiled-coil. The results showed significant differences in conformational stability between mutants containing trans-ACPC and cis-ACPC, despite differing only in one peripheral stereogenic center.

RSC ADVANCES (2022)

Review Biochemistry & Molecular Biology

Getting Closer to Decrypting the Phase Transitions of Bacterial Biomolecules

Katarzyna Soltys, Aneta Tarczewska, Dominika Bystranowska, Nikola Sozanska

Summary: Liquid-liquid phase separation is a new paradigm in cell biology and one of the mechanisms for the formation of membraneless organelles. Bacterial cells also undergo phase transitions and form structures resembling eukaryotic cellular condensates. This review provides an overview of microbial biomolecules that undergo liquid-liquid phase separation and the formation and organization of biomacromolecular condensates within cells. The challenges in investigating bacterial biomacromolecular condensates are discussed.

BIOMOLECULES (2022)

Article Cell Biology

Does one plus one always equal two? Structural differences between nesfatin-1,-2, and nesfatin-1/2

Rafal Lenda, Michal Padjasek, Artur Krezel, Andrzej Ozyhar, Dominika Bystranowska

Summary: This study analyzed the effect of Zn(II) and Ca(II) on the structure of human nesfatin-1, -2, and -1/2. The results revealed that human nesfatin-1 is an intrinsically disordered protein, while nesfatin-2 and nesfatin-1/2 have globular structures with intrinsically disordered regions. Zn(II) treatment led to structurization and compaction of nesfatin-1, as well as destabilization of nesfatin-2 and nesfatin-1/2. Furthermore, nesfatin-1 and -2 seemed to be interdependent when linked together, as the properties of nesfatin-1/2 were not a simple sum of the properties exhibited by the individual peptides.

CELL COMMUNICATION AND SIGNALING (2022)

Article Biochemistry & Molecular Biology

Deep blue autofluorescence reflects the oxidation state of human transthyretin

Elzbieta Wieczorek, Zofia Wygralak, Sylwia Kedracka-Krok, Patrycja Bezara, Dominika Bystranowska, Piotr Dobryszycki, Andrzej Ozyhar

Summary: TTR is a protein that transports thyroid hormones and retinol and functions as a neuro-protective factor and sensor of oxidative stress. This study found that the stability of TTR is influenced by calcium ions and other factors, resulting in the formation of blue autofluorescent compounds. The redox state of TTR affects the dynamics and properties of these compounds.

REDOX BIOLOGY (2022)

Review Biochemistry & Molecular Biology

The Role of Intrinsically Disordered Proteins in Liquid-Liquid Phase Separation during Calcium Carbonate Biomineralization

Aneta Tarczewska, Klaudia Bielak, Anna Zoglowek, Katarzyna Soltys, Piotr Dobryszycki, Andrzej Ozyhar, Miroslawa Rozycka

Summary: Some animal organs contain mineralized tissues, mainly deposits of calcium salts. Ear stones in the inner ear are essential for maintaining body balance. Intrinsically disordered proteins play a significant role in shaping and sizing otoliths.

BIOMOLECULES (2022)

Article Biochemistry & Molecular Biology

Effect of Gel Exposition on Calcium and Carbonate Ions Determines the Stm-l Effect on the Crystal Morphology of Calcium Carbonate

Miroslawa O. Rozycka, Klaudia Bielak, Maciej Ptak, Benjamin Jost, Gabriela Melo Rodriguez, Joachim Schoelkopf, Jaroslaw Stolarski, Piotr Dobryszycki, Andrzej Ozyhar

Summary: The biomineralization of fish otoliths is regulated by macromolecules, such as proteins, particularly intrinsically disordered proteins like the Starmaker-like protein. Bioinspired mineralization experiments were conducted to investigate the effects of this protein on calcium carbonate biominerals, considering prior exposure to calcium or carbonate ions. The presence of the Starmaker-like protein significantly affected the morphology and protein distribution within the crystals, highlighting the importance of environmental conditions on its action.

BIOMACROMOLECULES (2023)

Article Cell Biology

Nesfatin-3 possesses divalent metal ion binding properties, which remain hidden in the nucleobindin-2 precursor protein

Anna Skorupska-Stasiak, Dominika Bystranowska, Jozef Ba Tran, Artur Krezel, Andrzej Ozyhar

Summary: This study investigated the structural and biochemical properties of the C-terminal half of Nucb2 and found that its product, nesfatin-3, had completely different properties from its precursor protein. Despite their similarities, nesfatin-3 is likely to play different roles in physiological processes and have different effects on tissue function, metabolism, and its regulation. The results of this study clearly demonstrated that nesfatin-3 possesses divalent metal ion binding properties that were not found in the nucleobindin-2 precursor protein.

CELL COMMUNICATION AND SIGNALING (2023)

Article Chemistry, Physical

The application of the hierarchical approach for the construction of foldameric peptide self-assembled nanostructures

Monika Szefczyk, Natalia Szulc, Marlena Gasior-Glogowska, Dominika Bystranowska, Andrzej Zak, Andrzej Sikora, Oliwia Polanska, Andrzej Ozyhar, Lukasz Berlicki

Summary: In this paper, a hierarchical approach for constructing nanofibrils based on alpha,beta-peptide foldamers is proposed as a rational method for designing novel self-assembled nanomaterials. The incorporation of a specific amino acid residue resulted in the formation of helical foldamers, which was confirmed by spectroscopic techniques. The obtained alpha,beta-peptides showed a strong tendency to aggregate and form self-assembled nanostructures, as revealed by assays and microscopy. The location of the beta-amino acid in the coiled-coil structure affected the secondary structure and morphology of the self-assembled nanostructures.

SOFT MATTER (2023)

Article Biochemistry & Molecular Biology

Nucleobindin-2 consists of two structural components: The Zn2+-sensitive N-terminal half, consisting of nesfatin-1 and -2, and the Ca2+-sensitive C-terminal half, consisting of nesfatin-3

Dominika Bystranowska, Anna Skorupska, Katarzyna Soltys, Michal Padjasek, Artur Krezel, Andrzej Zak, Magdalena Kaus-Drobek, Michal Taube, Maciej Kozak, Andrzej Ozyhar

Summary: Studies show that binding of Mg2+ leads to changes in oligomerization state of Nucb2 with no significant structural alterations, while binding of Zn2+ has a more pronounced effect on the structure of Nucb2, causing local destabilization at the N-terminal half and inducing changes within the C-terminal half, resulting in oligomerization and/or aggregation of Nucb2 molecules. The results help to elucidate the structure of Nucb2, which can be divided into two parts: the Zn2+-sensitive N-terminal half and the Ca2+-sensitive C-terminal half, opening up new discussions on the roles of metal cations in regulating the structure and physiological functions of Nucb2.

COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL (2021)

Article Biochemistry & Molecular Biology

TPE conjugated islet amyloid polypeptide probe for detection of peptide oligomers

Hsiao-Chieh Tsai, Ching-Hong Huang, Ling-Hsien Tu

Summary: Islet amyloid polypeptide (IAPP) is a polypeptide hormone co-secreted with insulin by pancreatic beta-cells. It tends to aggregate into soluble oligomers, which are considered one of the hallmarks of type II diabetes. This study successfully grafted the aggregation-induced emission molecule TPE onto IAPP, allowing real-time monitoring of IAPP oligomer formation and potential application in the diagnosis of T2D.

BIOPHYSICAL CHEMISTRY (2024)

Article Biochemistry & Molecular Biology

Thermally stabilized chondroitin sulfate-hemoglobin nanoparticles and their interaction with bioactive compounds

Aristeidis Papagiannopoulos, Aggeliki Sklapani, Nikolaos Spiliopoulos

Summary: This study presents a method for preparing Hb-based nanoparticles (NPs) using a fully biocompatible approach. These NPs have a spherical structure with a diameter ranging from 50 to 100 nm, and can form electrostatic complexes with CS at pH 4. The NPs can be pH-tunable and stable in solutions with high salt content, making them suitable for nanodelivery of nutrients and drugs.

BIOPHYSICAL CHEMISTRY (2024)

Article Biochemistry & Molecular Biology

Osmotic stress studies of G-protein-coupled receptor rhodopsin activation

Andrey V. Struts, Alexander V. Barmasov, Steven D. E. Fried, Kushani S. K. Hewage, Suchithranga M. D. C. Perera, Michael F. Brown

Summary: This article summarizes and reviews the osmotic stress studies of G-protein-coupled receptor rhodopsin. It is found that water plays an important role in the activation of the receptor, with at least 80 water molecules entering the receptor in the transition to the active state. If water influx is prevented, the functional transition of the receptor is reversed. These findings reveal the phenomenon of solvent swelling in the activation mechanism of rhodopsin, with water acting as an allosteric modulator of function for rhodopsin-like receptors in lipid membranes.

BIOPHYSICAL CHEMISTRY (2024)

Article Biochemistry & Molecular Biology

Palmitoylation modifies transmembrane adaptor protein PAG for ordered lipid environment: A molecular dynamics simulation study

Maria Chiara Saija, Adela Melcrova, Wojciech Pajerski, Itay Schachter, Matti Javanainen, Marek Cebecauer, Lukasz Cwiklik

Summary: We used molecular dynamics simulations to investigate the effects of palmitoylation on a transmembrane peptide in different lipid environments. The study found that palmitoylation reduces the peptide's impact on membrane thickness, particularly in lipid-ordered and boundary environments. The hydrophobic palmitoyl chains on the peptide did not significantly affect membrane hydration. Interestingly, the boundary membrane environment was found to be highly compatible with the palmitoylated peptide. These findings have important implications for understanding cell signaling, membrane organization, and optimizing lipid membrane-based drug delivery systems.

BIOPHYSICAL CHEMISTRY (2024)

Article Biochemistry & Molecular Biology

Pomegranate peel, chokeberry leaves and Ironwort extract as novel natural inhibitors of amylin aggregation and cellular toxicity in pancreatic β cells

Achanta Rishisree, Brayer Mallory, Karnaukhova Elena, Jankovic Teodora, Zdunic Gordana, Savikin Katarina, Jeremic Aleksandar

Summary: Pomegranate peel, ironwort, and chokeberry leaf extracts exhibit anti-aggregative and antitoxic properties against human amylin. They can prevent amyloidosis and cell loss in patients with Type 2 Diabetes Mellitus.

BIOPHYSICAL CHEMISTRY (2024)