In the process of optimization of heterologous expression of thermostable chemotaxis proteins CheW and CheY as industrially useful polypeptides, their direct influence on the cell growth kinetics and morphology of Escherichia coli was observed. CheW and CheY of bacteria of the genus Thermotoga, being expressed in recombinant form in E. coli cells, are involved in the corresponding signal pathways of the mesophilic microorganisms. The effects of such involvement in the metabolism of “host” cells are extremely diverse: from rapid aging of the culture to elongation of the stationary growth phase. We also discuss the mechanisms of the influence of the heterologous chemotaxis proteins on cells, their positive and negative effects, as well as potential applications in industry and biomedicine.
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Grishin DV, Zhdanov DD, Gladilina YA, Podobed OV, Pokrovsky VS, Pokrovskaya MV, Aleksandrova SS, Sokolov NN. Thermostable Recombinant Polypeptides as the Source of L-Amino Acids for Culture Media. Bull. Exp. Biol. Med. 2018;165(4):461-464.
Grishin DV, Zhdanov DD, Gladilina JA, Pokrovsky VS, Podobed OV, Pokrovskaya MV, Aleksandrova SS, Milyushkina AL, Vigovskiy MA, Sokolov NN. Construction and characterization of a recombinant mutant homolog of the CheW protein from Thermotoga petrophila RKU-1. Biomed. Khim. 2018;64(1):53-60.
Alexandre G, Zhulin IB. Different evolutionary constraints on chemotaxis proteins CheW and CheY revealed by heterologous expression studies and protein sequence analysis. J. Bacteriol. 2003;185(2):544-552.
Boukhvalova MS, Dahlquist FW, Stewart RC. CheW binding interactions with CheA and Tar: importance for chemotaxis signaling in Escherichia coli. J. Biol. Chem. 2002;277(25):22 251-22 259.
Drury L. Transformation of bacteria by electroporation.. Methods Mol. Biol. 1996;58:249-256.
Gibson DG. Enzymatic assembly of overlapping DNA fragments. Methods Enzymol. 2011;498:349-361.
Lee SY, Cho HS, Pelton JG, Yan D, Henderson RK, King DS, Huang L, Kustu S, Berry EA, Wemmer DE. Crystal structure of an activated response regulator bound to its target. Nat. Struct. Biol. 2001;8(1):52-56.
Oleskin AV, Botvinko .V, Tsavkelova EA. Colonial organization and intercellular communication in microorganisms. Mikrobiologiia. 2000;69(3):309-327.
Silversmith RE, Smith JG, Guanga GP, Les JT, Bourret RB. Alteration of a nonconserved active site residue in the chemotaxis response regulator CheY affects phosphorylation and interaction with CheZ. J. Biol. Chem. 2001;276(21):18,478-18,484.
Sourjik V, Berg HC. Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol. Microbiol. 2000;37(4):740-751.
Zhao R, Collins EJ, Bourret RB, Silversmith RE. Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Nat. Struct. Biol. 2002;9(8):570-575.
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 167, No. 3, pp. 351-355, March, 2019
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Grishin, D.V., Samoilenko, V.A., Gladilina, Y.A. et al. Effect of Heterologous Expression of Chemotaxis Proteins from Genus Thermotoga on the Growth Kinetics of Escherichia coli Cells. Bull Exp Biol Med 167, 375–379 (2019). https://doi.org/10.1007/s10517-019-04530-z
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DOI: https://doi.org/10.1007/s10517-019-04530-z