| Orginal Article |
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| Advances in Bacterial Adaptive Evolution under Heavy Metal Ion Stress |
MA Chun-lan,LI Jin-hua,BAI Yu-fan,WEI Yun-lin( ) |
| Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming 650500, China |
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Abstract Base mutation, gene re-arrangement or horizontal gene transfer are the fundamental mechanisms involved in bacterial evolution. During adaptive evolution, they are mainly affected by biological and abiological factors. Among them, heavy metal ion stress is also one of the main reasons during bacterial adaptive evolution, and it drives bacteria to adaptively strengthen the metabolic pathways related to metal input and/or transformation. On the other hand, excessive metal ion also can induce metal accumulation and efflux. Under heavy metal stress, heavy metal resistance (HMR) gene and enzyme protein play an important role involved in mechanisms of bacterial adaptive evolution. The mechanisms include the adaptation of isolation, the regulatory adaptation of metal regulatory protein and the adaptation of enzyme detoxification. The current research status and progress were summarized in this paper. Heavy metal ions have polluted the environment and threatened human health and ecosystem stability. Therefore, to elucidate the molecular mechanisms of adaptive evolution of bacteria under heavy metal stress, this paper not only enriches the content of bacterial evolutionism, but also provides a theoretical basis for the biological remediation of environmental pollution by heavy metal ions.
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Received: 30 August 2021
Published: 03 March 2022
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Corresponding Authors:
Yun-lin WEI
E-mail: homework18@126.com
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| [1] |
Ruan L W, Lin W Y, Shi H, et al. Characterization of a novel extracellular CuZn superoxide dismutase from Rimicaris exoculata living around deep-sea hydrothermal vent. International Journal of Biological Macromolecules, 2020(163):2346-2356.
|
|
|
| [2] |
张亚男, 宋娜, 徐丽, 等. CD109的生物学功能及其与乳腺癌的关系. 中华细胞与干细胞杂志(电子版), 2019, 9(3):182-187.
|
|
|
| [2] |
Zhang Y N, Song N, Xu L, et al. Biological function of CD109 and its relationship with breast cancer. Chinese Journal of Cell and Stem Cell (Electronic Edition), 2019, 9(3):182-187.
|
|
|
| [3] |
Cheng Y Q, Yang R J, Lyu M Y, et al. IdeR, a DtxR family iron response regulator, controls iron homeostasis, morphological differentiation, secondary metabolism, and the oxidative stress response in Streptomyces avermitilis. Applied and Environmental Microbiology, 2018, 84(22):e01503-e01518.
|
|
|
| [4] |
Liu Q, Song W Z, Zhou Y G, et al. Phenotypic divergence of thermotolerance: molecular basis and cold adaptive evolution related to intrinsic DNA flexibility of glacier-inhabiting Cryobacterium strains. Environmental Microbiology, 2020, 22(4):1409-1420.
doi: 10.1111/emi.v22.4
|
|
|
| [5] |
Chandrangsu P, Rensing C, Helmann J D. Metal homeostasis and resistance in bacteria. Nature Reviews Microbiology, 2017, 15(6):338-350.
doi: 10.1038/nrmicro.2017.15
pmid: 28344348
|
|
|
| [6] |
Presentato A, Piacenza E, Turner R J, et al. Processing of metals and metalloids by actinobacteria: cell resistance mechanisms and synthesis of metal(loid)-based nanostructures. Microorganisms, 2020, 8(12):2027.
doi: 10.3390/microorganisms8122027
|
|
|
| [7] |
Daisley B A, Monachese M, Trinder M, et al. Immobilization of cadmium and lead by Lactobacillus rhamnosus GR-1 mitigates apical-to-basolateral heavy metal translocation in a Caco-2 model of the intestinal epithelium. Gut Microbes, 2019, 10(3):321-333.
doi: 10.1080/19490976.2018.1526581
|
|
|
| [8] |
Kalidasan V, Joseph N, Kumar S, et al. Iron and virulence in Stenotrophomonas maltophilia: all we know so far. Frontiers in Cellular and Infection Microbiology, 2018, 8:401.
doi: 10.3389/fcimb.2018.00401
pmid: 30483485
|
|
|
| [9] |
Zeng F R, Zahoor M, Waseem M, et al. Influence of metal-resistant Staphylococcus aureus strain K1 on the alleviation of chromium stress in wheat. Agronomy, 2020, 10(9):1354.
doi: 10.3390/agronomy10091354
|
|
|
| [10] |
León-Torres A, Arango E, Castillo E, et al. CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis. Biological Research, 2020, 53(1):6.
doi: 10.1186/s40659-020-00274-7
pmid: 32054527
|
|
|
| [11] |
Srivastava J, Chandra H, Singh N, et al. Understanding the development of environmental resistance among microbes: a review. CLEAN - Soil, Air, Water, 2016, 44(7):901-908.
doi: 10.1002/clen.v44.7
|
|
|
| [12] |
Eriksen R S, Krishna S. Defence versus growth in a hostile world: lessons from phage and bacteria. Royal Society Open Science, 2020, 7(9):201118.
doi: 10.1098/rsos.201118
|
|
|
| [13] |
Hampton H G, Smith L M, Ferguson S, et al. Functional genomics reveals the toxin-antitoxin repertoire and AbiE activity in Serratia. Microbial Genomics, 2020, 6(11):mgen000458.
|
|
|
| [14] |
Rostøl J T, Marraffini L. (Ph)ighting phages: how bacteria resist their parasites. Cell Host & Microbe, 2019, 25(2):184-194.
|
|
|
| [15] |
Derry W B. CRISPR: development of a technology and its applications. The FEBS Journal, 2021, 288(2):358-359.
doi: 10.1111/febs.v288.2
|
|
|
| [16] |
Brovedan M A, Cameranesi M M, Limansky A S, et al. What do we know about plasmids carried by members of the Acinetobacter genus? World Journal of Microbiology & Biotechnology, 2020, 36(8):109.
doi: 10.1007/s11274-020-02890-7
|
|
|
| [17] |
Shi-Kunne X, van Kooten M, Depotter J R L, et al. The genome of the fungal pathogen Verticillium dahliae reveals extensive bacterial to fungal gene transfer. Genome Biology and Evolution, 2019, 11(3):855-868.
doi: 10.1093/gbe/evz040
pmid: 30799497
|
|
|
| [18] |
Jaramillo V D, Sukno S A, Thon M R. Identification of horizontally transferred genes in the genus Colletotrichum reveals a steady tempo of bacterial to fungal gene transfer. BMC Genomics, 2015, 16(1):2.
doi: 10.1186/1471-2164-16-2
|
|
|
| [19] |
Rezzoagli C, Granato E T, Kümmerli R. Harnessing bacterial interactions to manage infections: a review on the opportunistic pathogen Pseudomonas aeruginosa as a case example. Journal of Medical Microbiology, 2020, 69(2):147-161.
doi: 10.1099/jmm.0.001134
pmid: 31961787
|
|
|
| [20] |
Martinez J L. General principles of antibiotic resistance in bacteria. Drug Discovery Today: Technologies, 2014, 11:33-39.
doi: 10.1016/j.ddtec.2014.02.001
pmid: 24847651
|
|
|
| [21] |
Li L Z, Liu Z H, Zhang M, et al. Insights into the metabolism and evolution of the genus Acidiphilium, a typical acidophile in acid mine drainage. mSystems, 2020, 5(6):e00867-20.
|
|
|
| [22] |
Aktuganov G E, Galimzianova N F, Gilvanova E A, et al. Characterization of chitinase produced by the alkaliphilic Bacillus mannanilyticus IB-OR17 B1 strain. Applied Biochemistry and Microbiology, 2018, 54(5):505-511.
doi: 10.1134/S0003683818050022
|
|
|
| [23] |
Koivulehto M, Battchikova N, Korpela S, et al. Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria. Open Chemistry, 2020, 18(1):149-164.
doi: 10.1515/chem-2020-0014
|
|
|
| [24] |
Millacura F A, Janssen P J, Monsieurs P, et al. Unintentional genomic changes endow Cupriavidus metallidurans with an augmented heavy-metal resistance. Genes, 2018, 9(11):551.
doi: 10.3390/genes9110551
|
|
|
| [25] |
王伟. 恶臭假单胞菌CD2 P型ATP酶基因cadA1抗Zn2+功能的确定. 武汉: 华中农业大学, 2008.
|
|
|
| [25] |
Wang W. Determination of Zn2+-resistant function of P-type ATPase gene cadA1 in Pseudomonas putida CD2. Wuhan: Huazhong Agricultural University, 2008.
|
|
|
| [26] |
Dai M X, Zhou G Q, Ng H Y, et al. Diversity evolution of functional bacteria and resistance genes (CzcA) in aerobic activated sludge under Cd(II) stress. Journal of Environmental Management, 2019, 250:109519.
doi: 10.1016/j.jenvman.2019.109519
|
|
|
| [27] |
Randazzo P, Anba-Mondoloni J, Aubert-Frambourg A, et al. Bacillus subtilis regulators MntR and zur participate in redox cycling, antibiotic sensitivity, and cell wall plasticity. Journal of Bacteriology, 2020, 202(5):e00547-e00519.
|
|
|
| [28] |
Harvie D R, Andreini C, Cavallaro G, et al. Predicting metals sensed by ArsR-SmtB repressors: allosteric interference by a non-effector metal. Molecular Microbiology, 2006, 59(4):1341-1356.
doi: 10.1111/mmi.2006.59.issue-4
|
|
|
| [29] |
Touchon M, Bernheim A, Rocha E P. Genetic and life-history traits associated with the distribution of prophages in bacteria. The ISME Journal, 2016, 10(11):2744-2754.
doi: 10.1038/ismej.2016.47
|
|
|
| [30] |
Vandecraen J, Monsieurs P, Mergeay M, et al. Zinc-induced transposition of insertion sequence elements contributes to increased adaptability of Cupriavidus metallidurans. Frontiers in Microbiology, 2016, 7:359.
doi: 10.3389/fmicb.2016.00359
pmid: 27047473
|
|
|
| [31] |
Zhang S H, Yang G L, Hou S G, et al. Analysis of heavy metal-related indices in the Eboling permafrost on the Tibetan Plateau. CATENA, 2021, 196:104907.
doi: 10.1016/j.catena.2020.104907
|
|
|
| [32] |
王敏. 嗜冷微生物对Cu2+胁迫的应答及其代谢组学研究. 哈尔滨: 哈尔滨工业大学, 2012.
|
|
|
| [32] |
Wang M. Stress responses and metabolomics under Cu2+ in psychrophilic microorganism. Harbin: Harbin Institute of Technology, 2012.
|
|
|
| [33] |
Alfano M, Cavazza C. Structure, function, and biosynthesis of nickel-dependent enzymes. Protein Science, 2020, 29(5):1071-1089.
doi: 10.1002/pro.v29.5
|
|
|
| [34] |
Chirgadze Y N, Boshkova E A, Battaile K P, et al. Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family. Journal of Biomolecular Structure & Dynamics, 2018, 36(2):376-386.
|
|
|
| [35] |
Kim J, Choi D, Cha S Y, et al. Zinc-mediated reversible multimerization of Hsp31 enhances the activity of holding chaperone. Journal of Molecular Biology, 2018, 430(12):1760-1772.
doi: 10.1016/j.jmb.2018.04.029
|
|
|
| [36] |
Raytapadar S, Datta R, Paul A K. Effects of some heavy metals on growth, pigment and antibiotic production by Streptomyces galbus. Acta Microbiologica et Immunologica Hungarica, 1995, 42(2):171-177.
pmid: 7551710
|
|
|
| [37] |
Remenár M, Karelová E, Harichová J, et al. Actinobacteria occurrence and their metabolic characteristics in the nickel-contaminated soil sample. Biologia, 2014, 69(11):1453-1463.
doi: 10.2478/s11756-014-0451-z
|
|
|
| [38] |
Caldeira J B, Chung A P, Morais P V, et al. Relevance of FeoAB system in Rhodanobacter sp. B2A1Ga4 resistance to heavy metals, aluminium, gallium, and indium. Applied Microbiology and Biotechnology, 2021, 105(8):3301-3314.
doi: 10.1007/s00253-021-11254-6
pmid: 33791837
|
|
|
| [39] |
Manley O M, Myers P D, Toney D J, et al. Evaluation of the regulatory model for Ni2+ sensing by Nur from Streptomyces coelicolor. Journal of Inorganic Biochemistry, 2020, 203:110859.
doi: 10.1016/j.jinorgbio.2019.110859
|
|
|
| [40] |
Baksh K A, Pichugin D, Prosser R S, et al. Allosteric regulation of the nickel-responsive NikR transcription factor from Helicobacter pylori. Journal of Biological Chemistry, 2021, 296:100069.
doi: 10.1074/jbc.RA120.015459
|
|
|
| [41] |
Lee C W, Giedroc D P. 1H, 13C, and 15N resonance assignments of NmtR, a Ni(II)/Co(II) metalloregulatory protein of Mycobacterium tuberculosis. Biomolecular NMR Assignments, 2013, 7(2):145-148.
doi: 10.1007/s12104-012-9397-7
|
|
|
| [42] |
Higgins K, Surette V, Swanson G, et al. Characterization of KmtR from Mycobacterium tuberculosis. Abstracts of Papers of the American Chemical Society, 2017, 254.
|
|
|
| [43] |
Bafana A, Khan F, Suguna K. Structural and functional characterization of mercuric reductase from Lysinibacillus sphaericus strain G1. BioMetals, 2017, 30(5):809-819.
doi: 10.1007/s10534-017-0050-x
pmid: 28894951
|
|
|
| [44] |
Kang W, Zheng J, Bao J G, et al. Characterization of the copper resistance mechanism and bioremediation potential of an Acinetobacter calcoaceticus strain isolated from copper mine sludge. Environmental Science and Pollution Research International, 2020, 27(8):7922-7933.
doi: 10.1007/s11356-019-07303-3
pmid: 31893366
|
|
|
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