E. Blochl, R. Rachel, S. Burggraf, D. Hafenbradl, H.W. Jannasch, K.O. Stetter, Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C, Extremophiles, 1 (1997) 14-21. DOI: 10.1007/s007920050010
K. Takai, K. Nakamura, T. Toki, U. Tsunogai, M. Miyazaki, J. Miyazaki, H. Hirayama, S. Nakagawa, T. Nunoura, K. Horikoshi, Cell proliferation at 122 degrees C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation, Proc. Natl. Acad. Sci. U.S.A., 105 (2008) 10949-10954. DOI: 10.1073/pnas.0712334105
Y. Yang, W. Zhao, X. Xiao, The upper temperature limit of life under high hydrostatic pressure in the deep biosphere, Deep-Sea Res. I, 176 (2021) 103604. DOI: 10.1016/j.dsr.2021.103604
K. Junge, H. Eicken, J.W. Deming, Bacterial Activity at -2 to -20 degrees C in Arctic wintertime sea ice, Appl. Environ. Microbiol., 70 (2004) 550-557. DOI: 10.1128/AEM.70.1.550-557.2004
N.C. Mykytczuk, S.J. Foote, C.R. Omelon, G. Southam, C.W. Greer, L.G. Whyte, Bacterial growth at -15 degrees C; molecular insights from the permafrost bacterium Planococcus halocryophilus Or1, The ISME journal, 7 (2013) 1211-1226. DOI: 10.1038/ismej.2013.8
S. Kumar, R. Nussinov, How do thermophilic proteins deal with heat?, Cell. Mol. Life Sci., 58 (2001) 1216-1233. DOI: 10.1007/PL00000935
K.A. Luke, C.L. Higgins, P. Wittung-Stafshede, Thermodynamic stability and folding of proteins from hyperthermophilic organisms, FEBS J., 274 (2007) 4023-4033. DOI: 10.1111/j.1742-4658.2007.05955.x
C. Vieille, G.J. Zeikus, Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability, Microbiol. Mol. Biol. Rev., 65 (2001) 1-43. DOI: 10.1128/MMBR.65.1.1-43.2001
T. Collins, G. Feller, Psychrophilic enzymes: strategies for cold-adaptation, Essays Biochem., 67 (2023) 701-713. DOI: 10.1042/EBC20220193
G. Feller, Protein folding at extreme temperatures: Current issues, Semin. Cell. Dev. Biol., 84 (2018) 129-137. DOI: 10.1016/j.semcdb.2017.09.003
Y. Zhang, C. Bao, L. Shen, C. Tian, X. Zang, G. Chen, S. Zhang, Microbial cold shock proteins: Overview of their function and mechanism of action, Protein Pept. Lett., 29 (2022) 133-142. DOI: 10.2174/0929866528666211118084519
Y. Zhang, C.A. Gross, Cold shock response in bacteria, Annu. Rev. Genet., 55 (2021) 377-400. DOI: 10.1146/annurev-genet-071819-031654
L. Giaquinto, P.M.G. Curmi, K.S. Siddiqui, A. Poljak, E. DeLong, S. DasSarma, R. Cavicchioli, Structure and function of cold shock proteins in archaea, J. Bacteriol., 189 (2007) 5738-5748. DOI: 10.1128/JB.00395-07
D. Wassenberg, C. Welker, R. Jaenicke, Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima, J. Mol. Biol., 289 (1999) 187-193. DOI: 10.1006/jmbi.1999.2772
D. Perl, C. Welker, T. Schindler, K. Schroder, M.A. Marahiel, R. Jaenicke, F.X. Schmid, Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins, Nat. Struct. Biol., 5 (1998) 229-235. DOI: 10.1038/nsb0398-229
Z. Xue, H. Sun, H. Hong, Z. Zhang, Y. Zhang, Z. Guo, S. Le, H. Chen, Comparative analysis of folding and unfolding dynamics and free-energy landscapes in homologous cold shock proteins with variable thermal stabilities, Phys. Rev. Res., 6 (2024) 023170. DOI: 10.1103/PhysRevResearch.6.023170
Y. Lee, C. Kwak, K.W. Jeong, P. Durai, K.S. Ryu, E.H. Kim, C. Cheong, H.C. Ahn, H.J. Kim, Y. Kim, Tyr51: Key determinant of the low thermostability of the Colwellia psychrerythraea cold-shock protein, Biochemistry, 57 (2018) 3625-3640. DOI: 10.1021/acs.biochem.8b00144
W. Feng, R. Tejero, D.E. Zimmerman, M. Inouye, G.T. Montelione, Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site, Biochemistry, 37 (1998) 10881-10896. DOI: 10.1021/bi980269j
W. Kremer, B. Schuler, S. Harrieder, M. Geyer, W. Gronwald, C. Welker, R. Jaenicke, H.R. Kalbitzer, Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima, Eur. J. Biochem., 268 (2001) 2527-2539. DOI: 10.1046/j.1432-1327.2001.02127.x
C. Medigue, E. Krin, G. Pascal, V. Barbe, A. Bernsel, P.N. Bertin, F. Cheung, S. Cruveiller, S. D'Amico, A. Duilio, G. Fang, G. Feller, C. Ho, S. Mangenot, G. Marino, J. Nilsson, E. Parrilli, E.P. Rocha, Z. Rouy, A. Sekowska, M.L. Tutino, D. Vallenet, G. von Heijne, A. Danchin, Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125, Genome research, 15 (2005) 1325-1335. DOI: 10.1101/gr.4126905
W. Qi, A. Colarusso, M. Olombrada, E. Parrilli, A. Patrignani, M.L. Tutino, M. Toll-Riera, New insights on Pseudoalteromonas haloplanktis TAC125 genome organization and benchmarks of genome assembly applications using next and third generation sequencing technologies, Sci. Rep., 9 (2019) 16444. DOI: 10.1038/s41598-019-52832-z
H. Latif, J.A. Lerman, V.A. Portnoy, Y. Tarasova, H. Nagarajan, A.C. Schrimpe-Rutledge, R.D. Smith, J.N. Adkins, D.H. Lee, Y. Qiu, K. Zengler, The genome organization of Thermotoga maritima reflects its lifestyle, PLoS genetics, 9 (2013) e1003485. DOI: 10.1371/journal.pgen.1003485
H. Schagger, Tricine-SDS-PAGE, Nat. Protoc., 1 (2006) 16-22. DOI: 10.1038/nprot.2006.4
A. Matouschek, J.M. Matthews, C.M. Johnson, A.R. Fersht, Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions, Protein Eng., 7 (1994) 1089-1095. DOI: 10.1093/protein/7.9.1089
G. Feller, Protein stability and enzyme activity at extreme biological temperatures, J. Phys. Condens. Matter, 22 (2010) 323101. DOI:10.1088/0953-8984/22/32/323101
A.S. Panja, B. Bandopadhyay, S. Maiti, Protein thermostability is owing to their preferences to non-polar smaller volume amino acids, variations in residual physico-chemical properties and more salt-bridges, PloS one, 10 (2015) e0131495. DOI: 10.1371/journal.pone.0131495
G. Feller, C. Gerday, Psychrophilic enzymes: hot topics in cold adaptation, Nat. Rev. Microbiol., 1 (2003) 200-208. DOI: 10.1038/nrmicro773
P.L. Privalov, Stability of proteins: small globular proteins, Adv. Protein Chem., 33 (1979) 167-241. DOI: 10.1016/s0065-3233(08)60460-x
J.K. Myers, C.N. Pace, J.M. Scholtz, Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding, Protein Sci., 4 (1995) 2138-2148. DOI: 10.1002/pro.5560041020
W.J. Becktel, J.A. Schellman, Protein stability curves, Biopolymers, 26 (1987) 1859-1877. DOI: 10.1002/bip.360261104
S. Kumar, R. Nussinov, Experiment-guided thermodynamic simulations on reversible two-state proteins: implications for protein thermostability, Biophys. Chem., 111 (2004) 235-246. DOI: 10.1016/j.bpc.2004.06.005
S. Kumar, C.J. Tsai, R. Nussinov, Maximal stabilities of reversible two-state proteins, Biochemistry, 41 (2002) 5359-5374. DOI: 10.1021/bi012154c
J.A. Schellman, Temperature, stability, and the hydrophobic interaction, Biophys J, 73 (1997) 2960-2964. DOI: 10.1016/S0006-3495(97)78324-3
G.I. Makhatadze, P.L. Privalov, Energetics of protein structure, Adv. Protein. Chem., 47 (1995) 307-425. DOI: 10.1016/s0065-3233(08)60548-3
G. Feller, D. d'Amico, C. Gerday, Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis, Biochemistry, 38 (1999) 4613-4619. DOI: 10.1021/bi982650+
C. Struvay, S. Negro, A. Matagne, G. Feller, Energetics of protein stability at extreme environmental temperatures in bacterial trigger factors, Biochemistry, 52 (2013) 2982-2990. DOI: 10.1021/bi4002387
G. Feller, Life at low temperatures: is disorder the driving force? Extremophiles, 11 (2007) 211-216. DOI: 10.1007/s00792-006-0050-1
S. D'Amico, J.C. Marx, C. Gerday, G. Feller, Activity-stability relationships in extremophilic enzymes, J. Biol. Chem., 278 (2003) 7891-7896. DOI: 10.1074/jbc.M212508200
D. Perl, U. Mueller, U. Heinemann, F. X. Schmid, Two exposed amino acid residues confer thermostability on a cold shock protein, Nat. Struct. Biol., 7 (2000) 380-383. DOI: 10.1038/75151