The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii

Vishnyakov, Innokentii E.; Bogachev, Mikhail I.; Салафутдинов, И. И.; Borchsenius, S.N.; Kayumov, Airat R.

doi:10.1007/s12668-016-0259-0

Cited by 6 publications

(3 citation statements)

References 21 publications

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“…The molecular weight, isoelectric point, aliphatic index, charge, hydropathy, and instability index of proteins have been calculated using and tools. Next, the distributions of the calculated physical and chemical properties for all proteins interacting with F105 in vivo and in vitro as well as the entire pattern obtained from the S. aureus genome were compared using statistical Kolmogorov-Smirnov test as previously [45].…”

Section: Methodsmentioning

confidence: 99%

Unraveling the Molecular Mechanism of Selective Antimicrobial Activity of 2(5H)-Furanone Derivative against Staphylococcus aureus

Sharafutdinov

Pavlova

Akhatova

et al. 2019

IJMS

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Staphylococcus aureus causes various infectious diseases, from skin impetigo to life-threatening bacteremia and sepsis, thus appearing an important target for antimicrobial therapeutics. In turn, the rapid development of antibiotic resistance and biofilm formation makes it extremely robust against treatment. Here, we unravel the molecular mechanism of the antimicrobial activity of the recently unveiled F105 consisting of three pharmacophores: chlorinated 2(5H)-furanone, sulfone, and l-menthol moieties. F105 demonstrates highly selective activity against Gram-positive bacteria and biofilm-embedded S. aureus and exhibits low risk of resistance development. We show explicitly that the fluorescent analogue of F105 rapidly penetrates into Gram-positive bacteria independently of their cell integrity and viability and accumulates there. By contrast, Gram-negative bacteria remain impermeable and, therefore, insusceptible to F105. Apparently, in bacterial cells, F105 induces reactive oxygen species (ROS) formation and nonspecifically interacts with a number of proteins, including ROS-utilizing ones. Using native and 2D PAGE, we confirm that F105 changes the charge of some proteins by either oxidation or direct interaction with them. Therefore, it seems justified to conclude that being simultaneously a ROS inducer and damaging proteins responsible for ROS utilization, F105 impairs the cellular anti-ROS defense representing a prospective ROS-inducing antibacterial agent.

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Section: Methodsmentioning

confidence: 99%

Unraveling the Molecular Mechanism of Selective Antimicrobial Activity of 2(5H)-Furanone Derivative against Staphylococcus aureus

Sharafutdinov

Pavlova

Akhatova

et al. 2019

IJMS

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“…Another example of membrane-less organelle formed transiently and only during the stress response is the so-called granular body found in mycoplasma Acholeplasma laidlawii [ 184 , 185 ]. A. laidlawii granular bodies form in response to heat shock and contain a small heat shock protein, IbpA, which has a subset of interacting partners [ 186 ] and assembles into globular-type oligomers and fibrils [ 187 ]. A. laidlawii belongs to Mollicutes, a class of microorganisms that possess the smallest known genome sizes among autonomously replicating organisms [ 188 ] and, thus, developed highly evolutionary optimized gene regulatory networks and metabolic pathways.…”

Section: Prokaryotesmentioning

confidence: 99%

Reorganization of Cell Compartmentalization Induced by Stress

et al. 2022

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The discovery of intrinsically disordered proteins (IDPs) that do not have an ordered structure and nevertheless perform essential functions has opened a new era in the understanding of cellular compartmentalization. It threw the bridge from the mostly mechanistic model of the organization of the living matter to the idea of highly dynamic and functional "soft matter". This paradigm is based on the notion of the major role of liquid-liquid phase separation (LLPS) of biopolymers in the spatial-temporal organization of intracellular space. The LLPS leads to the formation of self-assembled membrane-less organelles (MLOs). MLOs are multicomponent and multifunctional biological condensates, highly dynamic in structure and composition, that allow them to fine-tune the regulation of various intracellular processes. IDPs play a central role in the assembly and functioning of MLOs. The LLPS importance for the regulation of chemical reactions inside the cell is clearly illustrated by the reorganization of the intracellular space during stress response. As a reaction to various types of stresses, stress-induced MLOs appear in the cell, enabling the preservation of the genetic and protein material during unfavourable conditions. In addition, stress causes structural, functional, and compositional changes in the MLOs permanently present inside the cells. In this review, we describe the assembly of stress-induced MLOs and the stress-induced modification of existing MLOs in eukaryotes, yeasts, and prokaryotes in response to various stress factors.

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“…40,41 In vitro AlIbpA was shown to exhibit the chaperone-like activity by preventing the DTT-or heat-induced aggregation of insulin 40 as well as of various cellular proteins from E. coli and A. laidlawii itself. 42,43 In the following we unravel the roles of both N-and C-terminal regions of AlIbpA for self-oligomerization, substrate binding and the chaperone function regulation. Our data indicate that Nterminus behaves as an auto-inhibitor and activity regulator of the C-terminus which in turn is required for the chaperone function and protein oligomerization in brillar form.…”

Section: Introductionmentioning

confidence: 99%

N- and C-terminal regions of the small heat shock protein IbpA from Acholeplasma laidlawii competitively govern its oligomerization pattern and chaperone-like activity

et al. 2020

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The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii

Cited by 6 publications

References 21 publications

Unraveling the Molecular Mechanism of Selective Antimicrobial Activity of 2(5H)-Furanone Derivative against Staphylococcus aureus

Unraveling the Molecular Mechanism of Selective Antimicrobial Activity of 2(5H)-Furanone Derivative against Staphylococcus aureus

Reorganization of Cell Compartmentalization Induced by Stress

N- and C-terminal regions of the small heat shock protein IbpA from Acholeplasma laidlawii competitively govern its oligomerization pattern and chaperone-like activity

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