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PubMed1979

Spectroscopic forms of carbonmonoxi-cytochrome oxidase.

A systematic study of the errors of low-temperature recording of kinetics of the cytochrome oxidase-CO reaction had identified the classic devitrification process of Keilin & Hartree [(1950) Nature (London)165, 504-505]. The methodology described here minimizes this effect, and the computation methods afford appropriate ways of detecting a residual effect. Thus it has been possible to identify that absorption difference spectra and kinetics of the reaction of fully reduced or half-reduced cytochrome oxidase with CO indicate only one spectroscopic form of the respective carbonmonoxi-cytochrome oxidase.

Animals↗

PubMed1977

Primary photochemical event in vision: proton translocation.

Picosecond studies of rhodopsin in low-temperature glasses have been carried out in order to observe directly the risetime of prelumirhodopsin, the first intermediate in the visual pathway. Only at 20 K or below can the risetime of this intermediate be resolved and even at 4 K it is astoundingly rapid, about 36 psec. An examination of the Arrhenius dependence on temperature of the rate of formation of prelumirhodopsin shows a strong deviation from linearity at low temperatures, i.e., non-Arrhenius behavior. This marked non-linear behavior is characteristic of a quantum mechanical tunneling event such as the translocation of hydrogen. An excellent candidate for the tunnelling process is the hydrogen of the protonated Schiff base formed between opsin and its retinal chromophore. Deuterium-exchanged rhodopsin, in which the Schiff base hydrogen is replaced by a deuterium, also shows a marked non-Arrhenius temperature dependence at low temperatures, consistent with tunneling. The rate of formation of prelumirhodopsin in deuterium-exchanged samples is much slower and a deuterium isotope effect kH/kD approximately or equal to 7 is observed. The data support a model in which the formation of prelumirhodopsin involves translocation of a proton toward the Schiff base nitrogen of the retinal chromophore.

Animals↗

PubMed1977

Temperature-dependent changes of chloride transport kinetics in human red cells.

Chloride self-exchange in human red cells was studied between 0 degrees C and 38 degrees C. At higher temperatures the flow-tube method was used. Although the general features of chloride transport at 0 degrees C and 38 degrees C are similar, the following differences were found: (a) the maximum pH of chloride self-exchange flux was lowered 0.6 pH unit from 7.8 to 7.2 when temperature was increased from 0 degrees C to 38 degrees C; (b)the apparent half-saturation constant increased from 28 mM at 0 degrees C to 65 mM at 38 degrees C; (c) chloride transport at body temperature is slower than predicted by other investigators by extrapolation from low-temperature results. Chloride transport increased only 200 times when temperature was raised from 0 degrees C to 38 degrees C, because the apparent activation energy decreased from 30 kcal mol(-1) to 20 kcal mol(-1) above a temperature of 15 degrees C; (d) a study of temperature dependence of the slower bromide self-exchange showed that a similar change of activation energy occurred around 25 degrees C. Both in the case of Cl(-) (15 degrees C) and in the case of Br(-) (25 degrees C), critical temperature was reached when the anion self-exchange had a turnover number of about 4x10(9) ions cell (-1)s(-1); (e) inhibition of chloride transport by DIDS (4,4'- diisothiocyano-stilbene-2,2'-disulfonate)revealed that the deflection persisted at 15 degrees C at partial inhibition (66 percent) presumably because DIDS inactivated 66 percent of the transport sites. It is suggested that a less temperature- dependent step of anion exchange becomes rate limiting at the temperature where a critical turnover number is reached.

Biological Transport↗

PubMed2025

Cross-species phenotypic profiling uncovers functional determinants of bacterial cold shock adaptation.

Temperature shifts impose broad physiological stress, requiring precise and dynamic regulatory programs to restore cellular homeostasis. While the heat shock response is well characterized, the mechanisms underlying cold shock response (CSR) remain less understood. To identify genes critical for cold adaptation, we applied transposon sequencing (Tn-seq) to monitor mutant fitness across the full course of CSR and sustained low-temperature growth in two mesophilic bacteria, Escherichia coli and Bacillus subtilis. In B. subtilis, phenotypic profiling revealed a temporally structured program: membrane fluidity and cell wall remodeling were most critical in the early stage of CSR, whereas post-transcriptional regulation became essential during late-stage recovery to reprogram gene expression and restore growth. Cross-species comparison uncovered both conserved and species-specific mechanisms, with RNA metabolism and ribosome/translation regulators playing broad roles. Specifically, we identified a conserved synergy between two ribosomal RNA methyltransferases, RsmA and RsmH, in promoting cold adaptation. In B. subtilis, mutants lacking these enzymes exhibited significant delay in translation recovery following cold-induced global inhibition. Together, these findings provide a comparative, systems-level view of bacterial cold adaptation and establish a framework for exploring stress responses in pathogens and extremophiles.

Cell envelope↗

PubMed1977

Ionization dependence of camphor binding and spin conversion of the complex between cytochrome P-450 and camphor. Kinetic and static studies at sub-zero temperatures.

The kinetic rate constants of formation and dissociation of the cytochrome-P-450 - camphor complex (Fe3+-RH) have been obtained by low-temperature (+ 5 degrees C to -20 degrees C) stopped-flow experiments. Simiarly the high-spin/low-spin equilibrium of this complex has been studied as a function of temperature and protonic activity. Both the camphor-binding mechanism and the high-spin/low-spin thermodynamic parameters of Fe3+-RH depend on the protonic activity of the medium in the physiological pH range. The binding rate constants are shown to depend on the ionization of a residue of the protein, probably a histidine. Linear enthalpy-entropy compensation is observed for the camphor binding as well as for the spin-state transition. A camphor-binding-induced change of the electrostatic potential is discussed.

Calorimetry↗

PubMed1979

Levels of asbestos air pollution in some environmental situations.

Asbestos contamination of the outside aid in Paris and suburbs has been monitored in some environmental situations, namely, "typical" urban sites removed from known sources of asbestos emissions, crossroad locations, the vicinity of a freeway, areas with buildings under construction, and areas around asbestos factories. In the same manner, measurements have been performed inside buildings of various types: those sprayed with asbestos-containing materials, those fitted with asbestos products, and control buildings. Air has been sampled by use of 0.45 micrometer pore size Millipore filters. After low-temperature ashing, ultrasonicated ashes were transferred to carbon film on 200-mesh gold grids examined under an analytic transmission electron microscope. Levels of pollution were expressed in terms of gravimetric concentrations. Inside buildings, when the air was in contact with significant amounts of asbestos-containing materials (spray, sheets), the levels were in the range 0.1--1000 10(-9) g m-3. In the vicinities of asbestos plants, the concentrations were higher: 1000--3000 10(-9) g m-3. Under other circumstances, the levels were of the same order of magnitude: 99% of the values were below 7 X 10(-9) g m-3. The Conseil Supérieur d'Hygiène Publique de France proposed a numerical ambient air quality standard of 50 X 10(-9) g m-3 inside buildings sprayed with asbestos.

Air Pollutants↗

PubMed2025

The chloroplast 16S rRNA dimethyltransferase BrPFC1 is required for Brassica rapa development under chilling stress.

Chloroplast ribosomal RNA (Ch-rRNA) methylation is critical for plant development and response to low temperatures. Several Ch-rRNA methyltransferases and their catalytic modes, as well as biological relevance, have been reported in model plant species. However, Ch-rRNA methyltransferases and their functional significance remain poorly characterized in crops, including leafy vegetables such as Chinese cabbage. In this study, we screened an EMS-mutagenized Chinese cabbage population and identified a yellow inner leaf (yif) mutant. This mutant develops yellowing inner leaves with reduced chlorophyll accumulation and ultrastructure-impaired chloroplasts under low-temperature conditions. Genetic analysis revealed a premature termination mutation in BrPFC1, encoding the chloroplast-localized 16S rRNA dimethyltransferase. The BrPFC1 mutation (yif) disrupts the dimethylation of 16S rRNA. The cold-sensitive phenotype of the yif mutant can be explained by temperature-dependent defects in the maturation and assembly of chloroplast ribosomes at 4°C. Through integrated analysis of chloroplast and nuclear transcriptomes coupled with translational profiling at 25°C and 4°C, we established that low temperature preferentially upregulates transcripts encoding nuclear-derived ribosomal proteins, while defective 16S rRNA specifically compromises the translational efficiency of chloroplast-encoded photosynthetic complex and ribosomal protein at 4°C. These findings establish rRNA modification by BrPFC1 as a critical regulatory layer for optimizing chloroplast translational efficiency at 4°C, providing mechanistic insights into post-translational adaptation strategies in Chinese cabbage.

Chloroplasts↗

PubMed1978

Sequence of b cytochromes relative to ubiquinone in the electron transport chain of Escherichia coli.

A ubiquinone-deficient mutant, carrying mutations in two genes affecting ubiquinone biosynthesis, has been used, in comparison with a normal strain, to determine the sequence of some of the components of the electron transport chain of Escherichia coli. The amounts of cytochromes reduced during aerobic steady-state conditions were estimated by comparing low-temperature difference spectra of normal or ubiquinone-deficient membranes with either D-lactate or reduced nicotinamide adenine dinucleotide as substrate. From the amounts of cytochromes reduced it was concluded that ubiquinone functions at two sites, one site being between the dehydrogenases and cytochromes and the second site being after cytochromes b562 and b556 but before cytochromes b558, d, and o. The scheme proposed is discussed in relation to the Mitchell protonmotive ubiquinone cycle.

Aerobiosis↗

PubMed1979

Augmented aftercontractions in papillary muscles from rats with cardiac hypertrophy.

Paired-pulse stimulation induced larger aftercontractions in papillary muscles from spontaneously hypertensive rats (SHR) than from normotensive Wistar-Kyoto rats (WKY). To determine whether aftercontraction exaggeration is a general characteristic of hypertrophied cardiac muscle, three models were examined: SHRs, deoxycorticosterone acetate (DOCA)-treated rats, and aorta-constricted rats. Responses of pipillary muscles from hypertrophied hearts tested under conditions conducive to aftercontraction generation were compared to pipillary muscles from WKY or sham-treated controls, respectively. Field-stimulated papillary muscles mounted in an oxygenated temperature-controlled physiologic salt solution were exposed to calcium concentrations of 2.5 and 5.0 mM, and temperatures of 27 degrees C and 17 degrees C. Although testing conditions influenced the contractile responses to single stimuli, there was no difference in active tension, time to peak tension, or one-half relaxation time between the three experimental groups and their respective controls. Paired-pulse stimulation induced aftercontractions that were enhanced in high-calcium and low-temperature solutions. Under these conditions, papillary muscles from hypertrophied hearts developed larger aftercontractions than did their respective controls.

Animals↗

PubMed1978

Effect of low temperature on growth, viability, and synthesis of mycolic acids of Mycobacterium tuberculosis strain H37Ra.

Cultures of Mycobacterium tuberculosis strain H37Ra were grownto early logarithmic phase at 37 degrees C and were incubated at 16 degrees, 20 degrees, and 25 degrees C. The decrease in this ability was more rapid at 20 degrees C than at 16 degrees C. Low-temperature incubation caused decreases in the ratios of mycolic acids and monounsaturated C16-19 fatty acids relative to the total of fatty acids synthesized. It also caused an increase in the ratio of saturated C24-26 fatty acids relative to the total of fatty acids synthesized. These ratios were based on the incorporation of radiolabel from 14C-acetate into fatty acids. These results showed that when M. tuberculosis H37Ra was incubated at low temperatures, it did not adapt by increasing the ratio of unsaturated to saturated fatty acids synthesized. The ability of the cells to synthesize mycolic acids was sharply decreased. These changes may lead to the loss of viability of M. tuberculosos H37Ra. Mycolic acid synthesis is similarly affected by exposure of cells to isoniazid, an antimycobacterial drug.

Chromatography, Thin Layer↗

PubMed2026

Integrative analysis of transcriptome and chromatin accessibility reveals promoter-proximal regulation and identifies candidate ABC transporters associated with cold stress responses in maize.

BACKGROUND: Low-temperature stress is a formidable environmental constraint that severely limits the growth and productivity of maize (Zea mays L.), particularly during the highly vulnerable early seedling stage. While cold tolerance is a critical agronomic objective, the integrated transcriptional and epigenetic regulatory mechanisms that govern this trait remain largely elusive. Characterizing these coordinated molecular networks is fundamental to the genetic enhancement of cold resilience in maize. METHODS: Using two maize inbred lines contrasting in chilling response (ZHB12 tolerant, B73 sensitive), we performed integrative time‑course RNA‑seq and ATAC‑seq to thoroughly and systematically characterize the precise dynamic interplay between gene expression and chromatin accessibility under cold stress conditions at the seedling stage. RESULTS: Physiological assessments confirmed that ZHB12 possesses superior cold tolerance, manifested by significantly attenuated electrolyte leakage and reduced foliar damage compared to B73. Transcriptomic profiling revealed a massive, time-dependent divergence in gene expression between the two genotypes, with a major regulatory transition identified at 24 h of cold exposure. Functional enrichment analysis demonstrated that ZHB12 preferentially activates a robust defense repertoire, including Photosystem II electron transport, diterpenoid biosynthesis, and ATP biosynthetic pathways. Notably, multiple ATP-binding cassette (ABC) transporter genes were coordinately upregulated under chilling, suggesting their potential involvement in cellular homeostasis. ATAC-seq analysis indicated that cold stress is associated with chromatin remodeling in ZHB12, with increased accessibility observed in proximal promoter regions. Integrative analysis identified a core set of dual-responsive genes, in which increased promoter accessibility coincided with transcriptional upregulation. These genes were predominantly enriched in transporter activity and transcriptional regulation, suggesting potential epigenetic link to the superior stress response of ZHB12. CONCLUSION: Our findings reveal extensive transcriptional and chromatin accessibility changes in ZHB12 under cold stress. The observed associations between promoter accessibility and gene activation, particularly in genes involved in transport processes, highlight candidate regulators potentially contributing to cold tolerance. This study provides a molecular framework and identifies high-value candidate genes that may inform future efforts in breeding cold-tolerant maize, pending functional validation.

Zea mays↗

PubMed2026

Genome-wide identification of WOX transcription factors and functional characterization of WOX4 and WOX13 involved in cold stress response in Malus baccata.

INTRODUCTION: Cold stress is a major abiotic threat to apple production. Malus baccata has exceptional cold hardiness and is widely used as a superior cold-resistant rootstock. The WUSCHEL-related homeobox (WOX) transcription factor family regulates plant growth, development and stress adaptation, whereas the functions of WOX genes in cold tolerance of M. baccata remain elusive. METHODS: In the present work, 19 MbWOX family members were identified and characterized at the genome-wide level. Evolutionary analysis, cis-element prediction, transcriptome profiling and real-time quantitative PCR (RT-qPCR) were performed to screen core cold-responsive genes. Overexpression vectors were constructed and transformed into Arabidopsis seedlings for functional verification. RESULTS: Evolutionary analysis revealed that segmental duplication drove the expansion of the MbWOX family, and these genes contained a variety of stress-responsive cis-elements. Combined transcriptome and RT-qPCR analyses confirmed that MbWOX4 and MbWOX13 were core cold-responsive genes with distinct expression patterns. The two genes participated in cold signal transduction by interacting with different transcription factor networks. Functional tests revealed that MbWOX4 and MbWOX13 isoforms differentially modulated seedling cold tolerance under low-temperature stress.

Malus baccata↗

PubMed2025

Integrated agronomy of pea (Pisum sativum L.): a review on cultivation, harvesting, and storage for sustainable agriculture.

Peas (Pisum sativum L.) are a cornerstone of sustainable agriculture, yet their potential is limited by fragmented agronomic practices. This review provides an integrated synthesis of advancements across cultivation, mechanized harvesting, and post-harvest storage. Key findings reveal that optimal growth conditions and nanotechnology interventions can significantly enhance abiotic stress tolerance. Mechanized harvesting innovations reduce yield losses by up to 40%, but smallholder adoption and terrain compatibility remain critical challenges. Effective post-harvest strategies, including low-temperature storage and hermetic bags, are crucial for preserving quality. Despite progress, systemic barriers persist. Future research must prioritize interdisciplinary solutions-combining genomics, precision engineering, and farmer training-to unlock the full potential of peas as a keystone crop for sustainable food systems.

climate resilience↗

PubMed2025

Genome-Wide Analysis of the AT-Hook Gene Family in Malus sieversii and Functional Characterization of MsAHL13.

AT-hook motif nuclear-localized (AHL) proteins are pivotal in plant growth, development, and stress responses. Nevertheless, there is limited research on AHL proteins in Malus sieversii. Our study identified 25 AHL genes from the M. sieversii genome, named MsAHL1-MsAHL25. The encoded protein sequences had lengths ranging from 195 to 554 amino acids, molecular weights from 19.17 to 58.53 kDa, and isoelectric points from 4.67 to 10.09. Chromosomal mapping revealed that these 25 genes were unevenly distributed across 10 chromosomes. Collinearity analysis of AHL genes in M. sieversii implied that gene loss might have occurred during its evolution. The phylogenetic tree classified the AHL proteins of M. sieversii into two subfamilies, showing a close relationship with multiple proteins of M. domestica. Promoter analysis indicated that the AHL genes in M. sieversii harbored numerous stress- and hormone-responsive elements, suggesting their potential role in various stress responses. qRT-PCR analysis of six representative MsAHLs under biotic and abiotic stresses demonstrated that the expression of MsAHL13, MsAHL15, and MsAHL17 was significantly upregulated under salt, drought, and cold stresses, while MsAHL01 expression was inhibited under low-temperature stress. All six MsAHLs were induced by the pathogen Valsa mali. Subcellular localization analysis of the specifically expressed protein MsAHL13 showed its nuclear location. Furthermore, luciferase and yeast two-hybrid assays confirmed the in vitro physical interaction between the MsAHL13 and MsMYB1 proteins. This research offers an important theoretical basis for further exploration of the functional mechanisms of this gene family in responding to environmental stresses.

Malus sieversii↗

PubMed2026

Physiological sub-typing of cold and freezing injury in Triticum turgidum subspecies with bioinformatic and expression characterization of glutathione reductase.

BACKGROUND: This study examined how different subspecies of Triticum turgidum (T. durum, T. polonicum, T. turanicum) respond to cold and freezing, assessing their water status, stress responses, and antioxidant system, with particular focus on the structure and function of glutathione reductase (TtGR). METHODS: TtGR genes were first identified from the T. turgidum genome using publicly available genomic resources such as Ensembl Plants. Promoter regions (~2 kb upstream) were analyzed to identify cis-regulatory elements using PlantCARE. Gene classification was performed based on predicted subcellular localization and conserved domain features. Plants were subjected to cold acclimation and freezing treatments, and physiological, biochemical, and enzymatic parameters were measured. RESULTS: Bioinformatics analyses identified four TtGR genes in the T. turgidum genome. The genes in two groups: cytosolic (Class I) and chloroplastic (Class II). Gene structure analysis showed a conserved exon-intron organization, while motif analysis confirmed the presence of Nicotinamide Adenine Dinucleotide Phosphate (NADPH)-binding and redox-active domains across all TtGR proteins. Several regulatory sequences in the promoters are involved in cold (DRE), abscisic acid (ABRE), and stress (STRE) responses, indicating that TtGR genes are dynamically regulated in response to environmental changes. Physiological analyses showed that freezing treatment reduces leaf water content in all genotypes, leading to turgor loss, hydrogen peroxide (H2O2) accumulation, and increased malondealdehyte (MDA) levels. However, tolerance mechanisms addressing water stress and membrane damage differ among genotypes. At the biochemical level, activation of the antioxidant defense system occurs in all genotypes. T. turanicum displays strong defense by significantly increasing enzyme activities, ensuring that the ascorbate-glutathione cycle continues under stress. By contrast, T. polonicum, although showing increased overall enzyme activities, experiences a dramatic drop in glutathione reductase (GR) activity at freezing temperatures, which restricts reduced glutathione (GSH) regeneration and creates a functional bottleneck in the antioxidant cycle. T. durum fails to sustain enzyme activities over the stress period, leading to an intermediate-sensitive response. Thus, whereas T. turanicum effectively maintains antioxidant function during freezing, T. polonicum and T. durum exhibit less efficient stress responses, either through enzymatic bottlenecks or a lack of sustained defense. CONCLUSIONS: One of the most striking findings of this study is the observed dissociation between TtGR gene expression levels and enzyme activities. Low temperature limits the link between transcription and enzyme function. The primary determinant of low-temperature tolerance in T. turgidum subspecies is the sustainability of GR enzyme activity and GSH regeneration under freezing conditions.

Triticum↗

PubMedDate not supplied

[Assessment of the quality of relcaimed water by total organic carbon].

The paper discusses possible application of the method of measuring the total content of organic carbon to evaluate the quality or reclaimed water. The paper gives data on the content of organic carbon, ratio of chemical consumption of oxygen and carbon in the atmospheric condensate, urine, condensate of urine low-temperature evaporation and portable water reclaimed from these sources.

Carbon↗

PubMed1977

The photochemical cycle of bacteriorhodopsin.

The reaction cycle of bacteriorhodopsin in the purple membrane isolated from Halobacterium halobium has been studied by optical absorption spectroscopy using low-temperature and flash kinetic techniques. After absorption of light, bacteriohodopsin passes through at least five distinct intermediates. The temperature and pH dependence of the absorbance changes suggests that branch points and/or reversible steps exist in this cycle. Flash spectroscopy in the presence of a pH-indicating dye shows that the transient release of a proton accompanies the photoreaction cycle. The proton release occurs from the exterior and the uptake is on the cytoplasmic side of the membrane, as required by the function of bacteriorhodopsin as a light-driven proton pump. Proton translocating steps connecting release and uptake are indicated by deuterium isotope effects on the kinetics of the cycle. The rapid decay of a light-induced linear dichroism shows that a chromophore orientation change occurs during the reaction cycle.

Bacteriorhodopsins↗

PubMed1979

[Electron acceptors in photosynthetic reaction centers from Rhodopseudomonas spheroides].

Using optical differential spectroscopy and EPR, a parallel study of light-induced electron transfer between the primary (X1) and secondary (X2) quinone-like acceptors in the preparations of reaction centers (RC) isolated from bacterial chromatophore membranes with sodium dodecyl sulfate was carried out. The data from direct measurements of the rate constant temperature dependence for the interaction between light-reduced X1 and X2 (KX1X2) are in good agreement with the data calculated from the kinetic analysis of dark reduction of photooxidized bacteriochlorophyll RC on the acceptors X1 and X2 (KX1X2 = 2.10(-1)S at 20 degrees; Ea = 11,8 kcal.mol-1 within the temperature range of 20 degrees-- -20 degrees). This evidence proves the efficiency of the previously used approach /1, 2/ for the evaluation of the X1-X2 interaction. The method proposed was used for a kinetic analysis of a low-temperature electron transfer from X1 to X2 in RC isolated with lauryldimethylaminoxide (KX1X2 = 2,3.10(2) S-1 at 20 degrees; Ea = 5,5 kcal.mol-1 within the temperature range of 10 degrees-- --70 degrees).

Bacterial Chromatophores↗