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Nonspecific stress response to temperature increase in Gammarus lacustris Sars with respect to oxygen-limited thermal tolerance concept / K. Vereshchagina [et al.] // PeerJ. - 2018. - Vol. 6. - Ст. e5571, DOI 10.7717/peerj.5571. - Cited References:49. - The study was carried out with the main financial support of Russian Science Foundation grant 17-14-01063, with the partial financial support of Russian Foundation for Basic Research grants 16-34-00687, 16-34-60060, 17-34-50012, the base part of Goszadanie project 6.9654.2017/8.9, joint program of DAAD and Ministry of education and Science M. Lomonosov (6.12735.2018/12.2) and Lake Baikal Foundation (FOB_02-3/05). There was no additional external funding received for this study. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 2167-8359

РУБ Multidisciplinary Sciences
Рубрики:
COPEPOD TIGRIOPUS-JAPONICUS
SHUNET SOUTH SIBERIA
HEAT-SHOCK PROTEINS
Кл.слова (ненормированные):
Gammarus lacustris -- Heat shock proteins 70 (HSP70) -- Nonspecific cellular -- stress-response (NCSR) -- Lactate dehydrogenase -- Diene conjugates -- Schiff -- bases -- Triene conjugates
Аннотация: The previously undescribed dynamics of the heat shock protein HSP70 and subsequent lipid peroxidation products have been assessed alongside lactate dehydrogenase activity for Gammarus lacustris Sars, an amphipod species from the saltwater Lake Shira (Republic of Khakassia). Individuals were exposed to a gradual temperature increase of 1 degrees C/hour (total exposure duration of 26 hours) starting from the mean annual temperature of their habitat (7 degrees C) up to 33 degrees C. A complex of biochemical reactions occurred when saltwater G. lactustris was exposed to the gradual changes in temperature. This was characterized by a decrease in lactate dehydrogenase activity and the launching of lipid peroxidation. The HSP70 level did not change significantly during the entire experiment. In agreement with the concept of oxygen-limited thermal tolerance, an accumulation of the most toxic lipid peroxides (triene conjugates and Schiff bases) in phospholipids occurred at the same time and temperature as the accumulation of lactate. The main criterion overriding the temperature threshold was, therefore, the transition to anaerobiosis, confirmed by the elevated lactate levels as observed in our previous associated study, and by the development of cellular stress, which was expressed by an accumulation of lipid peroxidation products. An earlier hypothesis, based on freshwater individuals of the same species, has been confirmed whereby the increased thermotolerance of G. lacustris from the saltwater lake was caused by differences in energy metabolism and energy supply of nonspecific cellular stress-response mechanisms. With the development of global climate change, these reactions could be advantageous for saltwater G. lacustris. The studied biochemical reactions can be used as biomarkers for the stress status of aquatic organisms when their habitat temperature changes.

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Держатели документа:
Irkutsk State Univ, Inst Biol, Irkutsk, Russia.
Baikal Res Ctr, Irkutsk, Russia.
Belarusian State Univ, Int Sakharov Environm Inst, Minsk, BELARUS.
SB RAS, Inst Biophys, Krasnoyarsk Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Vereshchagina, Kseniya; Kondrateva, Elizaveta; Axenov-Gribanov, Denis; Shatilina, Zhanna; Khomich, Andrey; Bedulina, Daria; Zadereev, Egor; Timofeyev, Maxim; Russian Science Foundation [17-14-01063]; Russian Foundation for Basic Research [16-34-00687, 16-34-60060, 17-34-50012]; Goszadanie project joint program of DAAD [6.9654.2017/8.9]; Ministry of education and Science M. Lomonosov [6.12735.2018/12.2]; Lake Baikal Foundation [FOB_02-3/05]

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Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class [Text] / S. . Bauer [et al.] // J. Mol. Biol. - 2004. - Vol. 339, Is. 4. - P. 967-979, DOI 10.1016/j.jmb.2004.04.034. - Cited References: 66 . - ISSN 0022-2836

РУБ Biochemistry & Molecular Biology
Рубрики:
GTP CYCLOHYDROLASE-I
   GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE
   6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE
   ESCHERICHIA-COLI
   DIHYDRONEOPTERIN ALDOLASE
   FOLIC-ACID
   ENZYMATIC SYNTHESIS
   DIHYDROPTEROATE SYNTHASE
   REACTION-MECHANISM
   3-DIMENSIONAL STRUCTURE
Кл.слова (ненормированные):
tetrahydrofolate biosynthesis -- aldolase classes -- retroaldol reaction -- purin binding -- Schiff base
Аннотация: Dihydroneopterin aldolase (DHNA) catalyses a retroaldol reaction yielding 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin, tetrahydrofolate. The enzyme is a potential target for antimicrobial and anti-parasite chemotherapy. A gene specifying a dihydroneopterin aldolase from Arabidopsis thaliana was expressed in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity and crystallised using polyethylenglycol as the precipitating agent. The crystal structure was solved by X-ray diffraction analysis at 2.2 Angstrom resolution. The enzyme forms a D-4-symmetric homo-octamer. Each polypeptide chain is folded into a single domain comprising an antiparallel four-stranded beta-sheet and two long alpha-helices. Four monomers are arranged in a tetrameric ring, and two of these rings form a hollow cylinder. Well defined purine derivatives are found at all eight topologically equivalent active sites. The subunit fold of the enzyme is related to substructures of dihydroneopterin triphosphate epimerase, GTP cyclohydrolase I, and pyruvoyltetrahydropterin synthase, which are all involved in the biosynthesis of pteridine type cofactors, and to urate oxidase, although some members of that superfamily have no detectable sequence similarity Due to structural and mechanistical differences of DHNA in comparison with class I and class II aldolases, a new aldolase class is proposed. (C) 2004 Elsevier Ltd. All rights reserved.

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Держатели документа:
Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
Tech Univ Munich, Lehrstuhl Organ Chem & Biochem, D-85747 Garching, Germany
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bauer, S...; Schott, A.K.; Illarionova, V...; Bacher, A...; Huber, R...; Fischer, M...

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