Journal articles: 'Cold adaptation'

1

Clarke, Andrew. "Cold adaptation." Journal of Zoology 225, no. 4 (December 1991): 691–99. http://dx.doi.org/10.1111/j.1469-7998.1991.tb04339.x.

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Budd, G. M. "Cold stress and cold adaptation." Journal of Thermal Biology 18, no. 5-6 (December 1993): 629–31. http://dx.doi.org/10.1016/0306-4565(93)90103-z.

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Kaur, Jaskiran, and Veena Khanna. "Bacterial Adaptation to Cold." International Journal of Current Microbiology and Applied Sciences 6, no. 11 (November 10, 2017): 628–35. http://dx.doi.org/10.20546/ijcmas.2017.611.075.

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Hayley, Michael, Tatiana Chevaldina, and David H. Heeley. "Cold Adaptation of Tropomyosin." Biochemistry 50, no. 30 (August 2, 2011): 6559–66. http://dx.doi.org/10.1021/bi200327g.

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Barria, C., M. Malecki, and C. M. Arraiano. "Bacterial adaptation to cold." Microbiology 159, Pt_12 (December 1, 2013): 2437–43. http://dx.doi.org/10.1099/mic.0.052209-0.

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Thieringer, Heather A., Pamela G. Jones, and Masayori Inouye. "Cold shock and adaptation." BioEssays 20, no. 1 (December 6, 1998): 49–57. http://dx.doi.org/10.1002/(sici)1521-1878(199801)20:1<49::aid-bies8>3.0.co;2-n.

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LEENANON, B., and M. A. DRAKE. "Acid Stress, Starvation, and Cold Stress Affect Poststress Behavior of Escherichia coli O157:H7 and Nonpathogenic Escherichia coli†." Journal of Food Protection 64, no. 7 (July 1, 2001): 970–74. http://dx.doi.org/10.4315/0362-028x-64.7.970.

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The effects of acid shock, acid adaptation, starvation, and cold stress of Escherichia coli O157:H7 (ATCC 43895), an rpo S mutant (FRIK 816-3), and nonpathogenic E. coli (ATCC 25922) on poststress heat resistance and freeze–thaw resistance were investigated. Following stress, heat tolerance at 56°C and freeze–thaw resistance at −20 to 21°C were determined. Heat and freeze–thaw resistance of E. coli O157:H7 and nonpathogenic E. coli was enhanced after acid adaptation and starvation. Following cold stress, heat resistance of E. coli O157:H7 and nonpathogenic E. coli was decreased, while freeze–thaw resistance was increased. Heat and freeze–thaw resistance of the rpoS mutant was enhanced only after acid adaptation. Increased or decreased tolerance of acid-adapted, starved, or cold-stressed E. coli O157:H7 cells to heat or freeze–thaw processes should be considered when processing minimally processed or extended shelf-life foods.

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TASARA, T., and R. STEPHAN. "Cold Stress Tolerance of Listeria monocytogenes: A Review of Molecular Adaptive Mechanisms and Food Safety Implications." Journal of Food Protection 69, no. 6 (June 1, 2006): 1473–84. http://dx.doi.org/10.4315/0362-028x-69.6.1473.

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The foodborne pathogen Listeria monocytogenes has many physiological adaptations that enable survival under a wide range of environmental conditions. The microbes overcome various types of stress, including the cold stress associated with low temperatures in food-production and storage environments. Cold stress adaptation mechanisms are therefore an important attribute of L. monocytogenes, enabling these food pathogens to survive and proliferate to reach minimal infectious levels on refrigerated foods. This phenomenon is a function of many molecular adaptation mechanisms. Therefore, an improved understanding of how cold stress is sensed and adaptation measures implemented by L. monocytogenes may facilitate the development of better ways of controlling these pathogens in food and related environments. Research over the past few years has highlighted some of the molecular aspects of cellular mechanisms behind cold stress adaptation in L. monocytogenes. This review provides an overview of the molecular and physiological constraints of cold stress and discusses the various cellular cold stress response mechanisms in L. monocytogenes, as well as their implications for food safety.

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BERRY, ELAINE D., and PEGGY M. FOEGEDING. "Cold Temperature Adaptation and Growth of Microorganisms†." Journal of Food Protection 60, no. 12 (December 1, 1997): 1583–94. http://dx.doi.org/10.4315/0362-028x-60.12.1583.

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Most microorganisms must accommodate a variety of changing conditions and stresses in their environment in order to survive and multiply. Because of the impact of temperature on all reactions of the cell, adaptations to fluctuations in temperature are possibly the most common. Widespread in the environment and well-equipped for cold temperature growth, psychrophilic and psychrotrophic microorganisms may yet make numerous adjustments when faced with temperatures lower than optimum. Phospholipid and fatty acid alterations resulting in increased membrane fluidity at lower temperatures have been described for many cold tolerant microorganisms while others may make no similar adjustment. While the enzymes of cold growing bacteria have been less extensively studied than those of thermophilic bacteria, it appears that function at low temperature requires enzymes with flexible conformational structure, in order to compensate for lower reaction rates. In many organisms, including psychrophilic and psychrotrophic bacteria, specific sets of cold shock proteins are induced upon abrupt shifts to colder temperatures. While this cold shock response has not been fully delineated, it appears to be adaptive, and may function to promote the expression of genes involved in translation when cells are displaced to lower temperatures. The cold shock response of Escherichia coli has been extensively studied, and the major cold shock protein CspA appears to be involved in the regulation of the response. Upon cold shock, the induction of CspA and its counterparts in most microorganisms studied is prominent, but transient; studies of this response in some psychrotrophic bacteria have reported constitutive synthesis and continued synthesis during cold temperature growth of CspA homologues, and it will be interesting to learn if these are common mechanisms of among cold tolerant organisms. Psychrotrophic microorganisms continue to be a spoilage and safety problem in refrigerated foods, and a greater understanding of the physiological mechanisms and implications of cold temperature adaptation and growth should enhance our ability to design more effective methods of preservation.

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Schade, Babette, Gregor Jansen, Malcolm Whiteway, Karl D. Entian, and David Y. Thomas. "Cold Adaptation in Budding Yeast." Molecular Biology of the Cell 15, no. 12 (December 2004): 5492–502. http://dx.doi.org/10.1091/mbc.e04-03-0167.

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We have determined the transcriptional response of the budding yeast Saccharomyces cerevisiae to cold. Yeast cells were exposed to 10°C for different lengths of time, and DNA microarrays were used to characterize the changes in transcript abundance. Two distinct groups of transcriptionally modulated genes were identified and defined as the early cold response and the late cold response. A detailed comparison of the cold response with various environmental stress responses revealed a substantial overlap between environmental stress response genes and late cold response genes. In addition, the accumulation of the carbohydrate reserves trehalose and glycogen is induced during late cold response. These observations suggest that the environmental stress response (ESR) occurs during the late cold response. The transcriptional activators Msn2p and Msn4p are involved in the induction of genes common to many stress responses, and we show that they mediate the stress response pattern observed during the late cold response. In contrast, classical markers of the ESR were absent during the early cold response, and the transcriptional response of the early cold response genes was Msn2p/Msn4p independent. This implies that the cold-specific early response is mediated by a different and as yet uncharacterized regulatory mechanism.

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Bertrand, Annick, and Yves Castonguay. "Plant adaptations to overwintering stresses and implications of climate change." Canadian Journal of Botany 81, no. 12 (December 1, 2003): 1145–52. http://dx.doi.org/10.1139/b03-129.

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Winter survival is a complex trait that does not solely rely on the plant's ability to withstand the direct effects of extreme cold temperatures. During long overwintering periods, plants are exposed to multiple abiotic (ice encasement, frost heave, desiccation, anoxia) and biotic (snow mould and other psychrophylic pathogens) stresses. Tolerance to these various stresses is based in part on shared adaptive traits and, consequently, cross-adaptation to environmental stresses is a key aspect of plant adaptation to cold. Increasing evidence of multiple functions for stress-induced proteins in overwintering plants confirms the need for a global approach in the analysis of adaptive mechanisms. From that perspective, the valorization of rapidly increasing knowledge on the molecular and genetic basis of plant and microbe adaptations to cold will demand multidisciplinary collaborations. Climate change will also need to be taken into account to identify the adaptive traits that will be required for agricultural and forest plants to survive winter in the future. More studies at the global and regional scales will be needed to assess the potential impact of climate warming on plant adaptation to winter and their interactions with low-temperature pathogens.Key words: cold adaptation, psychrophylic microorganisms, climate change, fall dormancy, low-temperature plantmicrobe interactions, cold-adaptation genomics.

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Daanen, Hein A. M., and Wouter D. Van Marken Lichtenbelt. "Human whole body cold adaptation." Temperature 3, no. 1 (January 2, 2016): 104–18. http://dx.doi.org/10.1080/23328940.2015.1135688.

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13

LeBlanc, J. "Mechanisms of Adaptation to Cold." International Journal of Sports Medicine 13, S 1 (October 1992): S169—S172. http://dx.doi.org/10.1055/s-2007-1024629.

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Åqvist, Johan. "Cold Adaptation of Triosephosphate Isomerase." Biochemistry 56, no. 32 (August 2, 2017): 4169–76. http://dx.doi.org/10.1021/acs.biochem.7b00523.

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Shigeo, Matsuno, Murakami Shigeki, Takagi Mitsuo, Hayashi Masami, Inouye Sakae, Hasegawa Ayako, and Fukai Konosuke. "Cold-adaptation of human rotavirus." Virus Research 7, no. 3 (May 1987): 273–80. http://dx.doi.org/10.1016/0168-1702(87)90033-5.

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16

Körner, Christian. "Plant adaptation to cold climates." F1000Research 5 (November 25, 2016): 2769. http://dx.doi.org/10.12688/f1000research.9107.1.

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In this short review, I will first summarize criteria by which environments can be considered “cold”, with plant stature (size, height above ground) playing a central role for the climate actually experienced. Plants adapted to such environments have to cope with both extremes and with gradual influences of low temperature. The first requires freezing resistance, which is tightly coupled to developmental state (phenology) and prehistory (acclimation). Gradual low temperature constraints affect the growth process (meristems) long before they affect photosynthetic carbon gain. Hence, plants growing in cold climates are commonly not carbon limited.

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Kim, Sun-Yong, Kwang Yeon Hwang, Sung-Hou Kim, Ha-Chin Sung, Ye Sun Han, and Yunje Cho. "Structural Basis for Cold Adaptation." Journal of Biological Chemistry 274, no. 17 (April 23, 1999): 11761–67. http://dx.doi.org/10.1074/jbc.274.17.11761.

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D'Amico, Salvino, Paule Claverie, Tony Collins, Daphné Georlette, Emmanuelle Gratia, Anne Hoyoux, Marie-Alice Meuwis, Georges Feller, and Charles Gerday. "Molecular basis of cold adaptation." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1423 (July 29, 2002): 917–25. http://dx.doi.org/10.1098/rstb.2002.1105.

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Cold–adapted, or psychrophilic, organisms are able to thrive at low temperatures in permanently cold environments, which in fact characterize the greatest proportion of our planet. Psychrophiles include both prokaryotic and eukaryotic organisms and thus represent a significant proportion of the living world. These organisms produce cold–evolved enzymes that are partially able to cope with the reduction in chemical reaction rates induced by low temperatures. As a rule, cold–active enzymes display a high catalytic efficiency, associated however, with a low thermal stability. In most cases, the adaptation to cold is achieved through a reduction in the activation energy that possibly originates from an increased flexibility of either a selected area or of the overall protein structure. This enhanced plasticity seems in turn to be induced by the weak thermal stability of psychrophilic enzymes. The adaptation strategies are beginning to be understood thanks to recent advances in the elucidation of the molecular characteristics of cold–adapted enzymes derived from X–ray crystallography, protein engineering and biophysical methods. Psychrophilic organisms and their enzymes have, in recent years, increasingly attracted the attention of the scientific community due to their peculiar properties that render them particularly useful in investigating the possible relationship existing between stability, flexibility and specific activity and as valuable tools for biotechnological purposes.

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19

Churchill, Steven Emilio. "Cold adaptation, heterochrony, and neandertals." Evolutionary Anthropology: Issues, News, and Reviews 7, no. 2 (1998): 46–60. http://dx.doi.org/10.1002/(sici)1520-6505(1998)7:2<46::aid-evan2>3.0.co;2-n.

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20

Panoff, Jean Michel. "Cold Shock Response and Adaptation." Cryobiology 42, no. 3 (May 2001): 222–23. http://dx.doi.org/10.1006/cryo.2001.2320.

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21

van Breukelen, Frank, and Sandra L. Martin. "Invited Review: Molecular adaptations in mammalian hibernators: unique adaptations or generalized responses?" Journal of Applied Physiology 92, no. 6 (June 1, 2002): 2640–47. http://dx.doi.org/10.1152/japplphysiol.01007.2001.

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Hibernators are unique among mammals in their ability to attain, withstand, and reverse low body temperatures. Hibernators repeatedly cycle between body temperatures near zero during torpor and 37°C during euthermy. How do these mammals maintain cardiac function, cell integrity, blood fluidity, and energetic balance during their prolonged periods at low body temperature and avoid damage when they rewarm? Hibernation is often considered an example of a unique adaptation for low-temperature function in mammals. Although such adaptation is apparent at the level of whole animal physiology, it is surprisingly difficult to demonstrate clear examples of adaptations at the cellular and biochemical levels that improve function in the cold and are unique to hibernators. Instead of adaptation for improved function in the cold, the key molecular adaptations of hibernation may be to exploit the cold to depress most aspects of biochemical function and then rewarm without damage to restore optimal function of all systems. These capabilities are likely due to novel regulation of biochemical pathways shared by all mammals, including humans.

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GIULIODORI, A. M. "Preferential translation of cold-shock mRNAs during cold adaptation." RNA 10, no. 2 (February 1, 2004): 265–76. http://dx.doi.org/10.1261/rna.5164904.

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23

Savourey, Gustave, Brigitte Barnavol, Jean-Pierre Caravel, Claude Feuerstein, and Jacques H. M. Bittel. "Hypothermic general cold adaptation induced by local cold acclimation." European Journal of Applied Physiology and Occupational Physiology 73, no. 3-4 (May 1996): 237–44. http://dx.doi.org/10.1007/bf02425482.

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24

Yamanaka, Kunitoshi, and Masayori Inouye. "Selective mRNA Degradation by Polynucleotide Phosphorylase in Cold Shock Adaptation in Escherichia coli." Journal of Bacteriology 183, no. 9 (May 1, 2001): 2808–16. http://dx.doi.org/10.1128/jb.183.9.2808-2816.2001.

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ABSTRACT Upon cold shock, Escherichia coli cell growth transiently stops. During this acclimation phase, specific cold shock proteins (CSPs) are highly induced. At the end of the acclimation phase, their synthesis is reduced to new basal levels, while the non-cold shock protein synthesis is resumed, resulting in cell growth reinitiation. Here, we report that polynucleotide phosphorylase (PNPase) is required to repress CSP production at the end of the acclimation phase. A pnp mutant, upon cold shock, maintained a high level of CSPs even after 24 h. PNPase was found to be essential for selective degradation of CSP mRNAs at 15°C. In a poly(A) polymerase mutant and a CsdA RNA helicase mutant, CSP expression upon cold shock was significantly prolonged, indicating that PNPase in concert with poly(A) polymerase and CsdA RNA helicase plays a critical role in cold shock adaptation.

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Zhang, Wei-Xin, Bin-Bin Xie, Xiu-Lan Chen, Sheng Dong, Xi-Ying Zhang, Bai-Cheng Zhou, and Yu-Zhong Zhang. "Domains III and I-2α, at the Entrance of the Binding Cleft, Play an Important Role in Cold Adaptation of the Periplasmic Dipeptide-Binding Protein (DppA) from the Deep-Sea Psychrophilic Bacterium Pseudoalteromonas sp. Strain SM9913." Applied and Environmental Microbiology 76, no. 13 (May 7, 2010): 4354–61. http://dx.doi.org/10.1128/aem.02884-09.

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ABSTRACT The peptide transporter from a cold-adapted bacterium has never been reported. In the present study, the dpp operon from the psychrophilic bacterium Pseudoalteromonas sp. strain SM9913 was cloned and analyzed. The dipeptide binding protein DppA of SM9913 was overexpressed in Escherichia coli, and its cold adaptation characteristics were studied. The recombinant DppA of SM9913 (PsDppA) displayed the highest ligand-binding affinity at 15°C, whereas the recombinant DppA of E. coli (EcDppA) displayed the highest ligand-binding affinity at 35°C. Thermal and guanidium hydrochloride unfolding analyses indicated that PsDppA has more structural instability than EcDppA. Six domain-exchanged mutants of PsDppA were expressed and purified. Analyses of these mutants indicated that domains III, I-2, and I-3 of PsDppA were less stable than those from EcDppA and that domains III and I-2 made a significant contribution to the high binding affinity of PsDppA at low temperatures. Structural and sequence analyses suggested that the state transition-involved regions in domain III and the α part of domain I-2 are the hot spots of optimization during cold adaptation and that decreasing the side-chain size in these regions is an important strategy for the cold adaptation of PsDppA.

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Castiglione, Gianni M., Frances E. Hauser, Brian S. Liao, Nathan K. Lujan, Alexander Van Nynatten, James M. Morrow, Ryan K. Schott, Nihar Bhattacharyya, Sarah Z. Dungan, and Belinda S. W. Chang. "Evolution of nonspectral rhodopsin function at high altitudes." Proceedings of the National Academy of Sciences 114, no. 28 (June 22, 2017): 7385–90. http://dx.doi.org/10.1073/pnas.1705765114.

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High-altitude environments present a range of biochemical and physiological challenges for organisms through decreases in oxygen, pressure, and temperature relative to lowland habitats. Protein-level adaptations to hypoxic high-altitude conditions have been identified in multiple terrestrial endotherms; however, comparable adaptations in aquatic ectotherms, such as fishes, have not been as extensively characterized. In enzyme proteins, cold adaptation is attained through functional trade-offs between stability and activity, often mediated by substitutions outside the active site. Little is known whether signaling proteins [e.g., G protein-coupled receptors (GPCRs)] exhibit natural variation in response to cold temperatures. Rhodopsin (RH1), the temperature-sensitive visual pigment mediating dim-light vision, offers an opportunity to enhance our understanding of thermal adaptation in a model GPCR. Here, we investigate the evolution of rhodopsin function in an Andean mountain catfish system spanning a range of elevations. Using molecular evolutionary analyses and site-directed mutagenesis experiments, we provide evidence for cold adaptation in RH1. We find that unique amino acid substitutions occur at sites under positive selection in high-altitude catfishes, located at opposite ends of the RH1 intramolecular hydrogen-bonding network. Natural high-altitude variants introduced into these sites via mutagenesis have limited effects on spectral tuning, yet decrease the stability of dark-state and light-activated rhodopsin, accelerating the decay of ligand-bound forms. As found in cold-adapted enzymes, this phenotype likely compensates for a cold-induced decrease in kinetic rates—properties of rhodopsin that mediate rod sensitivity and visual performance. Our results support a role for natural variation in enhancing the performance of GPCRs in response to cold temperatures.

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Erdal, Ufuk G., Zeynep K. Erdal, and Clifford W. Randall. "ADAPTATION OF EBPR BACTERIA TO COLD TEMPERATURE THROUGH HOMEOVISCOUS ADAPTATION." Proceedings of the Water Environment Federation 2002, no. 15 (January 1, 2002): 145–59. http://dx.doi.org/10.2175/193864702784247675.

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Igoshin, Alexander, Nikolay Yudin, Ruslan Aitnazarov, Andrey A. Yurchenko, and Denis M. Larkin. "Whole-Genome Resequencing Points to Candidate DNA Loci Affecting Body Temperature under Cold Stress in Siberian Cattle Populations." Life 11, no. 9 (September 13, 2021): 959. http://dx.doi.org/10.3390/life11090959.

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Despite the economic importance of creating cold resilient cattle breeds, our knowledge of the genetic basis of adaptation to cold environments in cattle is still scarce compared to information on other economically important traits. Herein, using whole-genome resequencing of animals showing contrasting phenotypes on temperature maintenance under acute cold stress combined with the existing SNP (single nucleotide polymorphism) functional annotations, we report chromosomal regions and candidate SNPs controlling body temperature in the Siberian cattle populations. The SNP ranking procedure based on regional FST calculations, functional annotations, and the allele frequency difference between cold-tolerant and cold-sensitive groups of animals pointed to multiple candidate genes. Among these, GRIA4, COX17, MAATS1, UPK1B, IFNGR1, DDX23, PPT1, THBS1, CCL5, ATF1, PLA1A, PRKAG1, and NR1I2 were previously related to thermal adaptations in cattle. Other genes, for example KMT2D and SNRPA1, are known to be related to thermogenesis in mice and cold adaptation in common carp, respectively. This work could be useful for cattle breeding strategies in countries with harsh climates, including the Russian Federation.

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Tang, Jie, Lian-Ming Du, Yuan-Mei Liang, and Maurycy Daroch. "Complete Genome Sequence and Comparative Analysis of Synechococcus sp. CS-601 (SynAce01), a Cold-Adapted Cyanobacterium from an Oligotrophic Antarctic Habitat." International Journal of Molecular Sciences 20, no. 1 (January 3, 2019): 152. http://dx.doi.org/10.3390/ijms20010152.

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Marine picocyanobacteria belonging to Synechococcus are major contributors to the global carbon cycle, however the genomic information of its cold-adapted members has been lacking to date. To fill this void the genome of a cold-adapted planktonic cyanobacterium Synechococcus sp. CS-601 (SynAce01) has been sequenced. The genome of the strain contains a single chromosome of approximately 2.75 MBp and GC content of 63.92%. Gene prediction yielded 2984 protein coding sequences and 44 tRNA genes. The genome contained evidence of horizontal gene transfer events during its evolution. CS-601 appears as a transport generalist with some specific adaptation to an oligotrophic marine environment. It has a broad repertoire of transporters of both inorganic and organic nutrients to survive in inhospitable environments. The cold adaptation of the strain exhibited characteristics of a psychrotroph rather than psychrophile. Its salt adaptation strategy is likely to rely on the uptake and synthesis of osmolytes, like glycerol or glycine betaine. Overall, the genome reveals two distinct patterns of adaptation to the inhospitable environment of Antarctica. Adaptation to an oligotrophic marine environment is likely due to an abundance of genes, probably acquired horizontally, that are associated with increased transport of nutrients, osmolytes, and light harvesting. On the other hand, adaptations to low temperatures are likely due to prolonged evolutionary changes.

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30

Yamashita, Michiaki. "Cold Adaptation of Fish Culture Cells." NIPPON SUISAN GAKKAISHI 63, no. 2 (1997): 251–52. http://dx.doi.org/10.2331/suisan.63.251.

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Pires, C. T. A., H. C. Ferreira, D. Uehara, and R. M. Sales. "ADAPTATION FOR TANDEM COLD MILL MODELS." IFAC Proceedings Volumes 40, no. 11 (2007): 293–98. http://dx.doi.org/10.3182/20070821-3-ca-2919.00044.

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Shephard, Roy J. "Adaptation to Exercise in the Cold." Sports Medicine 2, no. 1 (1985): 59–71. http://dx.doi.org/10.2165/00007256-198502010-00006.

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Saltykova, M. M. "PHYSIOLOGICAL MECHANISMS OF ADAPTATION TO COLD." Aerospace and Environmental Medicine 50, no. 4 (2016): 5–13. http://dx.doi.org/10.21687/0233-528x-2016-50-4-5-13.

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Ohman, M. "A Cold Editor Makes the Adaptation." Science 335, no. 6070 (February 16, 2012): 805–6. http://dx.doi.org/10.1126/science.1219300.

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35

Golden, F. S., and M. J. Tipton. "Human adaptation to repeated cold immersions." Journal of Physiology 396, no. 1 (February 1, 1988): 349–63. http://dx.doi.org/10.1113/jphysiol.1988.sp016965.

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Bjelic, Sinisa, Bjørn O. Brandsdal, and Johan Åqvist. "Cold Adaptation of Enzyme Reaction Rates†." Biochemistry 47, no. 38 (September 23, 2008): 10049–57. http://dx.doi.org/10.1021/bi801177k.

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Laurberg, P., S. Andersen, and J. Karmisholt. "Cold Adaptation and Thyroid Hormone Metabolism." Hormone and Metabolic Research 37, no. 9 (September 2005): 545–49. http://dx.doi.org/10.1055/s-2005-870420.

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Cartier, Gwendoline, Florence Lorieux, Frédéric Allemand, Marc Dreyfus, and Thierry Bizebard. "Cold Adaptation in DEAD-Box Proteins." Biochemistry 49, no. 12 (March 30, 2010): 2636–46. http://dx.doi.org/10.1021/bi902082d.

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Valledor, Luis, Takeshi Furuhashi, Anne-Mette Hanak, and Wolfram Weckwerth. "Systemic Cold Stress Adaptation ofChlamydomonas reinhardtii." Molecular & Cellular Proteomics 12, no. 8 (April 5, 2013): 2032–47. http://dx.doi.org/10.1074/mcp.m112.026765.

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Pires, Carlos Thadeu de Ávila, Henrique Cezar Ferreira, and Roberto Moura Sales. "Adaptation for tandem cold mill models." Journal of Materials Processing Technology 209, no. 7 (April 2009): 3592–96. http://dx.doi.org/10.1016/j.jmatprotec.2008.08.020.

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41

Steegmann, A. Theodore. "Human cold adaptation: An unfinished agenda." American Journal of Human Biology 19, no. 2 (2007): 218–27. http://dx.doi.org/10.1002/ajhb.20614.

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42

Wilhoft, Daniel C. "Cold Comfort Animal Adaptation to Cold L. C. H. Wang." BioScience 41, no. 1 (January 1991): 50–51. http://dx.doi.org/10.2307/1311544.

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43

Howe, Glenn T., Sally N. Aitken, David B. Neale, Kathleen D. Jermstad, Nicholas C. Wheeler, and Tony HH Chen. "From genotype to phenotype: unraveling the complexities of cold adaptation in forest trees." Canadian Journal of Botany 81, no. 12 (December 1, 2003): 1247–66. http://dx.doi.org/10.1139/b03-141.

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Adaptation to winter cold in temperate and boreal trees involves complex genetic, physiological, and developmental processes. Genecological studies demonstrate the existence of steep genetic clines for cold adaptation traits in relation to environmental (mostly temperature related) gradients. Population differentiation is generally stronger for cold adaptation traits than for other quantitative traits and allozymes. Therefore, these traits appear to be under strong natural selection. Nonetheless, high levels of genetic variation persist within populations. The genetic control of cold adaptation traits ranges from weak to strong, with phenological traits having the highest heritabilities. Within-population genetic correlations among traits range from negligible to moderate. Generally, bud phenology and cold hardiness in the fall are genetically uncorrelated with bud phenology and cold hardiness in the spring. Analyses of quantitative trait loci indicate that cold adaptation traits are mostly controlled by multiple genes with small effects and that quantitative trait loci × environment interactions are common. Given this inherent complexity, we suggest that future research should focus on identifying and developing markers for cold adaptation candidate genes, then using multilocus, multi allelic analytical techniques to uncover the relationships between genotype and phenotype at both the individual and population levels. Ultimately, these methods may be useful for predicting the performance of genotypes in breeding programs and for better understanding the evolutionary ecology of forest trees.Key words: association genetics, cold hardiness, dormancy, genecology, bud phenology, quantitative trait loci.

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Liu, Jing, Tianwei Liu, Yantao Liu, Yuzhen Wang, Liqin Liu, Li Gong, Bingjian Liu, and Zhenming Lü. "Comparative Transcriptome Analyses Provide New Insights into the Evolution of Divergent Thermal Resistance in Two Eel Gobies." Current Issues in Molecular Biology 46, no. 1 (December 25, 2023): 153–70. http://dx.doi.org/10.3390/cimb46010012.

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Adaptation to thermal conditions in tidal mudflats always involves tolerating frequent fluctuations and often extreme environmental temperatures. Regulation of gene expression plays a fundamental role in the evolution of these thermal adaptations. To identify the key gene regulatory networks associated with the thermal adaptation, we investigated the capability of cold tolerance, as well as the transcriptomic changes under cold stress in two mudflat inhabitants (Odontamblyopus lacepedii and O. rebecca) with contrasting latitude affinity. Our results revealed a remarkable divergent capacity of cold tolerance (CTmin: 0.61 °C vs. 9.57 °C) between the two gobies. Analysis of transcriptomic changes under cold stress unveiled 193 differentially expressed genes exhibiting similar expression profiles across all tissues and species, including several classic metabolic and circadian rhythm molecules such as ACOD and CIART that may represent the core cold response machinery in eel gobies. Meanwhile, some genes show a unique expression spectrum in the more cold-tolerant O. lacepedii suggesting their roles in the enhanced cold tolerance and hence the extreme thermal adaptations. In addition, a weighted gene co-expression network analysis (WGCNA) revealed a subset of metabolic hub genes including MYH11 and LIPT2 showing distinct down-regulation in O. lacepedii when exposed to cold stress which highlights the role of reduced energy consumption in the enhanced cold tolerance of eel gobies. These findings not only provide new insights into how mudflat teleosts could cope with cold stress and their potential evolutionary strategies for adapting to their thermal environment, but also have important implications for sound management and conservation of their fishery resources in a scenario of global climate warming in the marine realm.

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Deryabin, Alexander, Kseniya Zhukova, Natalia Naraikina, and Yuliya Venzhik. "Effect of Low Temperature on Content of Primary Metabolites in Two Wheat Genotypes Differing in Cold Tolerance." Metabolites 14, no. 4 (April 3, 2024): 199. http://dx.doi.org/10.3390/metabo14040199.

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The study of cold-tolerance mechanisms of wheat as a leading cereal crop is very relevant to science. Primary metabolites play an important role in the formation of increased cold tolerance. The aim of this research is to define changes in the content of primary metabolites (soluble proteins and sugars), growth, and photosynthetic apparatus of freezing-tolerant and cold-sustainable wheat (Triticum aestivum L.) genotypes under optimal conditions and after prolonged (7 days) exposure to low temperature (4 °C). In order to gain a deeper comprehension of the mechanisms behind wheat genotypes’ adaptation to cold, we determined the expression levels of photosynthetic genes (RbcS, RbcL) and genes encoding cold-regulated proteins (Wcor726, CBF14). The results indicated different cold-adaptation strategies of freezing-tolerant and cold-sustainable wheat genotypes, with soluble proteins and sugars playing a significant role in this process. In plants of freezing-tolerant genotypes, the strategy of adaptation to low temperature was aimed at increasing the content of soluble proteins and modification of carbohydrate metabolism. The accumulation of sugars was not observed in wheat of cold-sustainable genotypes during chilling, but a high content of soluble proteins was maintained both under optimal conditions and after cold exposure. The adaptation strategies of wheat genotypes differing in cold tolerance were related to the expression of photosynthetic genes and genes encoding cold-regulated proteins. The data improve our knowledge of physiological and biochemical mechanisms of wheat cold adaptation.

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Yurtaeva, E. Yu. "ANTIOXIDANT PROPERTIES OF CONVOLVULUS ARVENSIS IN ADAPTATION OF ORGANISM TO COLD." Amur Medical Journal, no. 3 (2017): 101–2. http://dx.doi.org/10.22448/amj.2017.3.101-102.

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KOLUPAEV, Yuriy, Tetiana YASTREB, Natalia RYABCHUN, Natalia KUZMYSHYNA, Mykola MARENYCH, and Viktor RYABCHUN. "Signaling and protection systems in the adaptation of plants to cold." Journal of Central European Agriculture 24, no. 1 (2023): 202–15. http://dx.doi.org/10.5513/jcea01/24.1.3776.

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Garnier, Matthieu, Sebastien Matamoros, Didier Chevret, Marie-France Pilet, Francoise Leroi, and Odile Tresse. "Adaptation to Cold and Proteomic Responses of the Psychrotrophic Biopreservative Lactococcus piscium Strain CNCM I-4031." Applied and Environmental Microbiology 76, no. 24 (October 8, 2010): 8011–18. http://dx.doi.org/10.1128/aem.01331-10.

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ABSTRACT There is considerable interest in the use of psychrotrophic bacteria for food biopreservation and in the understanding of cold adaptation mechanisms. The psychrotrophic biopreservative Lactococcus piscium strain CNCM I-4031 was studied for its growth behavior and proteomic responses after cold shock and during cold acclimation. Growth kinetics highlighted the absence of growth latency after cold shock, suggesting a very high promptness in cold adaptation, a behavior that has never been described before for lactic acid bacteria (LAB). A comparative proteomic analysis was applied with two-dimensional gel electrophoresis (2-DE), and upregulated proteins were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Both cold shock and cold acclimation triggered the upregulation of proteins involved in general and oxidative stress responses and fatty acid and energetic metabolism. However, 2-DE profiles and upregulated proteins were different under both conditions, suggesting a sequence of steps in cold adaptation. In addition, the major 7-kDa Csp protein was identified in the L. piscium CNCM I-4031 genome but was not cold regulated. The implication of the identified cold shock proteins and cold acclimation proteins in efficient cold adaptation, the possible regulation of a histidyl phosphocarrier protein, and the roles of a constitutive major 7-kDa Csp are discussed.

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Hüner, Norman P. A., Rainer Bode, Keshav Dahal, Florian A. Busch, Marc Possmayer, Beth Szyszka, Dominic Rosso, et al. "Shedding some light on cold acclimation, cold adaptation, and phenotypic plasticity." Botany 91, no. 3 (March 2013): 127–36. http://dx.doi.org/10.1139/cjb-2012-0174.

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In the past, the role of light as an energy source was largely ignored in research focused on cold acclimation and freezing tolerance in plants. However, cold acclimation is an energy-requiring process. We summarize research illustrating that photoautrophs as diverse as cyanobacteria (Plectonema boryanum), green algae (Chlorella vulgaris, Dunaliella salina, Chlamydomonas raudensis), crop plants (Triticum aestivum L., Secale cereale L., Brassica napus L.), and conifers (Pinus banksiana) L.) tailor the structure and function of the photosynthetic apparatus to changes in temperature and irradiance to maintain cellular energy balance called photostasis. Modulation of either temperature or irradiance results in a similar imbalance in cellular energy that is sensed through changes in chloroplastic excitation pressure. Thus, concepts of photostasis and excitation pressure provide the context through which one can explain the congruence of phenotypic plasticity and photosynthetic performance associated with cold acclimation and photoacclimation. Photosynthetic organisms can sense changes in temperature and irradiance through modulation of the redox state of the photosynthetic electron transport chain, which, in turn, governs phenotype through the regulation of nuclear gene expression and chloroplast biogenesis. We suggest that elucidation of the molecular mechanism(s) by which excitation pressure regulates phenotypic plasticity and photosynthetic performance will be essential in addressing the challenge of maintaining or perhaps enhancing crop productivity under the suboptimal growth conditions predicted to occur as a consequence of climate change.

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Williams, Caroline M., Marshall D. McCue, Nishanth E. Sunny, Andre Szejner-Sigal, Theodore J. Morgan, David B. Allison, and Daniel A. Hahn. "Cold adaptation increases rates of nutrient flow and metabolic plasticity during cold exposure in Drosophila melanogaster." Proceedings of the Royal Society B: Biological Sciences 283, no. 1838 (September 14, 2016): 20161317. http://dx.doi.org/10.1098/rspb.2016.1317.

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Metabolic flexibility is an important component of adaptation to stressful environments, including thermal stress and latitudinal adaptation. A long history of population genetic studies suggest that selection on core metabolic enzymes may shape life histories by altering metabolic flux. However, the direct relationship between selection on thermal stress hardiness and metabolic flux has not previously been tested. We investigated flexibility of nutrient catabolism during cold stress in Drosophila melanogaster artificially selected for fast or slow recovery from chill coma (i.e. cold-hardy or -susceptible), specifically testing the hypothesis that stress adaptation increases metabolic turnover. Using 13 C-labelled glucose, we first showed that cold-hardy flies more rapidly incorporate ingested carbon into amino acids and newly synthesized glucose, permitting rapid synthesis of proline, a compound shown elsewhere to improve survival of cold stress. Second, using glucose and leucine tracers we showed that cold-hardy flies had higher oxidation rates than cold-susceptible flies before cold exposure, similar oxidation rates during cold exposure, and returned to higher oxidation rates during recovery. Additionally, cold-hardy flies transferred compounds among body pools more rapidly during cold exposure and recovery. Increased metabolic turnover may allow cold-adapted flies to better prepare for, resist and repair/tolerate cold damage. This work illustrates for the first time differences in nutrient fluxes associated with cold adaptation, suggesting that metabolic costs associated with cold hardiness could invoke resource-based trade-offs that shape life histories.

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Journal articles on the topic 'Cold adaptation'

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