Anna Zoglowek

AGH University of Krakow

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Andrzej Ożyhar

Wrocław University of Science and Technology

Piotr Dobryszycki

Wrocław University of Science and Technology

Marek Orłowski

AGH University of Krakow

Grzegorz Rymarczyk

Proteostasis Therapeutics (United States)

Klaudia Bielak

Wrocław University of Science and Technology

Mirosława Różycka

Wrocław University of Science and Technology

Aneta Tarczewska

Wrocław University of Science and Technology

Szymon Pakuła

Wrocław University of Science and Technology

Joanna Pieprzyk

Centre for Structural Systems Biology

Tomasz Gwóźdź

Instytut Nauk Prawnych

Cooperative Institutions

Wrocław University of Science and Technology

AGH University of Krakow

Institute of Organic Chemistry

University of Wrocław

Polish Academy of Sciences

Yale University

University of Oxford

Institute of Physical Chemistry

Boston University

Brigham and Women's Hospital

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Proteins in Calcium Phosphates Biomineralization

IntechOpen eBooks (2019)

Marta Kalka Anna Zoglowek Andrzej Ożyhar Piotr Dobryczycki

Biomineralization is a process of creating crystalline structures under biological control. The process takes place in hard tissues, such as bones, cartilages, and teeth. Biominerals are a combination of a crystal phase deposited onto an organic matrix. Inorganic components are mainly responsible for the biomineral hardness, while the organic matrix controls the shape, size, and polymorph of the crystals. Within the organic matrix, proteins exhibit a special biomineralization activity. Among them, one can distinguish insoluble collagen and soluble noncollagenous proteins. It is particularly noteworthy that noncollagenous proteins are intrinsically disordered proteins. High flexibility, acidic nature, and susceptibility to modifications make them especially adapted to the biomineralization control. This review paper is dedicated to the proteins which are involved in biomineralization of bones and teeth.

Matrix (chemical analysis)

Mineralized tissues

10.5772/intechopen.86718

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Citations (6)

Structural Analyses of Ordered and Disordered Regions in Ecdysteroid Receptor

Springer eBooks (2015)

Marek Orłowski Piotr Dobryszycki Anna Zoglowek Joanna Pieprzyk K Bielska

Ecdysteroid

10.1007/978-3-319-18729-7_6

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Citations (1)

N′-terminal- and Ca2+-induced stabilization of high-order oligomers of full-length Danio rerio and Homo sapiens otolin-1

International Journal of Biological Macromolecules (2022)

Klaudia Bielak Rafał Hołubowicz Anna Zoglowek Andrzej Żak Paweł Kędzierski

Otolin-1 is a C1q family member and a major component of the organic matrix of fish otoliths and human otoconia. To date, the protein molecular properties have not been characterized. In this work, we describe biochemical characterization and comparative studies on saccular-specific otolin-1 derived from Danio rerio and Homo sapiens. Due to the low abundance of proteins in the otoconial matrix, we developed a production and purification method for both recombinant homologues of otolin-1. Danio rerio and Homo sapiens otolin-1 forms higher-order oligomers that can be partially disrupted under reducing conditions. The presence of Ca2+ stabilizes the oligomers and significantly increases the thermal stability of the proteins. Despite the high sequence coverage, the oligomerization of Danio rerio otolin-1 is more affected by the reducing conditions and presence of Ca2+ than the human homologue. The results show differences in molecular behaviour, which may be reflected in Danio rerio and Homo sapiens otolin-1 role in otolith and otoconia formation.

Danio

Homo sapiens

African clawed frog

10.1016/j.ijbiomac.2022.04.088

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Plasticity of the Ecdysone Receptor DNA Binding Domain

Molecular Endocrinology (2004)

Marek Orłowski Monika Szyszka Agnieszka Kowalska Iwona Grad Anna Zoglowek

Ecdysteroids coordinate molting and metamorphosis in insects via a heterodimer of two nuclear receptors, the ecdysone receptor (EcR) and the ultraspiracle (Usp) protein. Here we show how the DNA-recognition alpha-helix and the T box region of the EcR DNA-binding domain (EcRDBD) contribute to the specific interaction with the natural response element and to the stabilization of the EcRDBD molecule. The data indicate a remarkable mutational tolerance with respect to the DNA-binding function of the EcRDBD. This is particularly manifested in the heterocomplexes formed between the EcRDBD mutants and the wild-type Usp DNA-binding domain (UspDBD). Circular dichroism (CD) spectra and protein unfolding experiments indicate that, in contrast to the UspDBD, the EcRDBD is characterized by a lower alpha-helix content and a lower stability. As such, the EcRDBD appears to be an intrinsically unstructured protein-like molecule with a high degree of intramolecular plasticity. Because recently published crystal structures indicate that the ligand binding domain of the EcR is also characterized by the extreme adaptability, we suggest that plasticity of the EcR domains may be a key factor that allows a single EcR molecule to mediate diverse biological effects.

Ecdysone receptor

Helix (gastropod)

Hormone response element

10.1210/me.2004-0154

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Counter-Diffusion System as an in Vitro Model in the Investigation of Proteins Involved in the Formation of Calcium Carbonate Biominerals

Crystal Growth & Design (2021)

Klaudia Bielak Mirosława Różycka Anna Zoglowek Andrzej Ożyhar Piotr Dobryszycki

Mineralization in living organisms is highly regulated by the synergistic action of many macromolecules, where distinctive proteins play the role of direct modulators of the crystal growth. The number of methods for in vitro biomineralization studies in the presence of proteins is limited due to the influence of the environment on their functionality. We focus on a counter-diffusion system in the biomineralization of calcium carbonate that is based on the diffusion of salt solutions through a gel-matrix supplemented with the protein of interest. This article discusses the background of the system, physical principles, matrices commonly in use, advantages, limitations, variations, and our own experience. Special attention is paid to the overview of already published studies that applied the counter-diffusion system as a model for investigation of the biomineralization of calcium carbonate. The system has great potential to be widely used in the analysis of biomineralization-associated proteins in vitro and the biomineralization process itself. This perspective recalls the most important theoretical basis as well as practical application of the system for specialists in various fields of biomineralization.

10.1021/acs.cgd.0c01695

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

Biomolecules (2022)

Aneta Tarczewska Klaudia Bielak Anna Zoglowek Katarzyna Sołtys Piotr Dobryszycki

Some animal organs contain mineralized tissues. These so-called hard tissues are mostly deposits of calcium salts, usually in the form of calcium phosphate or calcium carbonate. Examples of this include fish otoliths and mammalian otoconia, which are found in the inner ear, and they are an essential part of the sensory system that maintains body balance. The composition of ear stones is quite well known, but the role of individual components in the nucleation and growth of these biominerals is enigmatic. It is sure that intrinsically disordered proteins (IDPs) play an important role in this aspect. They have an impact on the shape and size of otoliths. It seems probable that IDPs, with their inherent ability to phase separate, also play a role in nucleation processes. This review discusses the major theories on the mechanisms of biomineral nucleation with a focus on the importance of protein-driven liquid–liquid phase separation (LLPS). It also presents the current understanding of the role of IDPs in the formation of calcium carbonate biominerals and predicts their potential ability to drive LLPS.

Amorphous calcium carbonate

10.3390/biom12091266

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The composite nature of the interaction between nuclear receptors EcR and DHR38

Biological Chemistry (2012)

Anna Zoglowek Marek Orłowski Szymon Pakuła Joanna Dutko-Gwóźdź Dorota Pajdzik

Abstract Ecdysteroids coordinate essential biological processes in Drosophila through a complex of two nuclear receptors, the ecdysteroid receptor (EcR) and the ultraspiracle protein (Usp). Biochemical experiments have shown that, in contrast to Usp, the EcR molecule is characterized by high intramolecular plasticity. To investigate whether this plasticity is sufficient to form EcR complexes with nuclear receptors other than Usp, we studied the interaction of EcR with the DHR38 nuclear receptor. Previous in vitro experiments suggested that DHR38 can form complexes with Usp and thus disrupt Usp-EcR interaction with the specific hsp27pal response element. This article provides the experimental evidence that EcR is able to form complexes with DHR38 as well. The recombinant DNA-binding domains (DBDs) of EcR and DHR38 interact specifically on hsp27pal. However, the interaction between the receptors is not restricted to their isolated DBDs. We pre\xadsent data that indicate that the full-length EcR and DHR38 can also form specific complexes within the nuclei of living cells. This interaction is mediated by the hinge region of EcR, which was recently classified as an intrinsically disordered region. Our results indicate that DHR38 might modulate the activity of the Usp-EcR heterodimer by forming complexes with both of its components.

Ecdysteroid

Ecdysone receptor

10.1515/hsz-2011-0283

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Citations (12)

Conformational changes in the DNA-binding domains of the ecdysteroid receptor during the formation of a complex with the hsp27 response element

Journal of Biomolecular Structure and Dynamics (2012)

Szymon Pakuła Marek Orłowski Grzegorz Rymarczyk Tomasz Krusiński Michał Jakób

The ecdysone receptor (EcR) and the ultraspiracle protein (Usp) form the functional receptor for ecdysteroids that initiates metamorphosis in insects. The Usp and EcR DNA-binding domains (UspDBD and EcRDBD, respectively) form a heterodimer on the natural pseudopalindromic element from the hsp27 gene promoter. The conformational changes in the protein–DNA during the formation of the UspDBD-EcRDBD-hsp27 complex were analyzed. Recombined UspDBD and EcRDBD proteins were purified and fluorescein labeled (FL) using the intein method at the C-ends of both proteins. The changes in the distances from the respective C-ends of EcRDBD and/or UspDBD to the 5′- and/or 3′-end of the response element were measured using fluorescence resonance energy transfer (FRET) methodology. The binding of EcRDBD induced a strong conformational change in UspDBD and caused the C-terminal fragment of the UspDBD molecule to move away from both ends of the regulatory element. UspDBD also induced a significant conformational change in the EcRDBD molecule. The EcRDBD C-terminus moved away from the 5′-end of the regulatory element and moved close to the 3′-end. An analysis was also done on the effect that DHR38DBD, the Drosophila ortholog of the mammalian NGFI-B, had on the interaction of UspDBD and EcRDBD with hsp27. FRET analysis demonstrated that hsp27 bending was induced by DHR38DBD. Fluorescence data revealed that hsp27 had a shorter end-to-end distance both in the presence of EcRDBD as well as in the presence of EcRDBD together with DHR38DBD, with DNA bend angles of about 36.2° and 33.6°, respectively. A model of how DHR38DBD binds to hsp27 in the presence of EcRDBD is presented.

Ecdysteroid

10.1080/07391102.2012.682215

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Citations (5)