Bacterial metallothioneins

[1]Binz P.A., Kägi J.H.R.: Metallothionein: molecular evolution and classification (w) Metallothionein IV, red. Klaassen C.D. Springer, Basel 1999, s. 7–1310.1007/978-3-0348-8847-9_2Search in Google Scholar

[2]Bruins M.R., Kapil S., Oehme F.W.: Microbial resistance to metals in the environment. Ecotoxicol. Environ. Saf. 45, 198–207 (2000)Search in Google Scholar

[3]Blindauer C.A., Harrison M.D., Parkinson J.A., Robinson A.K., Cavet J.S., Robinson N.J., Sadler P.J.: A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity. Proc. Natl. Acad. Sci. USA, 98, 9593–9598 (2001)10.1073/pnas.171120098Search in Google Scholar

[4]Blindauer C.A., Harrison M.D., Robinson A.K., Parkinson J.A., Bowness P.W., Sadler P.J., Robinson N.J.: Multiple bacteria encode metallothioneins and SmtA-like zinc fingers. Mol. Microbiol. 45, 1421–1432 (2002)Search in Google Scholar

[5]Blindauer C.A., Sadler P.J.: How to hide zinc in a small protein. Acc. Chem. Res. 38, 62–69 (2005)Search in Google Scholar

[6]Blindauer C.A.: Bacterial metallothioneins (w) Metallothioneins and related chelators. Metal ions in life science vol. 5, red. Sigel A., Sigel H., Sigiel R.K.O. Royal Society of Chemistry, Cambridge 2009, s. 51–8110.1039/9781847559531-00051Search in Google Scholar

[7]Blindauer C.A.: Bacterial metallothioneins: past, present, and questions for the future. J. Biol. Inorg. Chem. 16, 1011–1024 (2011)Search in Google Scholar

[8]Busenlehner L.S., Pennella M.A., Giedroc D.P.: The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 27, 131–143 (2003)10.1016/S0168-6445(03)00054-8Search in Google Scholar

[9]Capdevila M., Atrian S.: Metallothionein protein evolution: a miniassay. J. Biol. Inorg. Chem. 16, 977–989 (2011)Search in Google Scholar

[10]Capdevila M., Bofill R., Palacios Ò., Atrian S.: State-of-art of metallothioneins at the beginning of the 21^st century. Coord. Chem. Rev. 256, 46–62 (2012)Search in Google Scholar

[11]Cavet J.S., Meng W., Pennella M.A., Appelhoff R.J., Giedroc D.P., Robinson N.J.: A nickel-cobalt sensing ArsR-SmtB family repressor: contributions of cytosol and effector binding sites to metal selectivity. J. Biol. Chem. 277, 38441–38448 (2002)Search in Google Scholar

[12]Clemens S.: Toxic metal accumulation, responses to exposure and mechanisms of tolerance in plants. Biochimie, 88, 1707–1719 (2006)10.1016/j.biochi.2006.07.00316914250Search in Google Scholar

[13]Dąbrowska G., Mierek-Adamska A., Goc A.: Characteristics of Brassica napus L. metallothionein genes: expression in organs and during seed germination. Austr. J. Crops Sci. 7, 1324–1332 (2013)Search in Google Scholar

[14]Daniels M.J., Turner-Cavet J.S., Selkirk R., Sun H., Parkinson J.A., Sadler P.J., Robinson N.J.: Coordination of Zn²⁺ (and Cd²⁺) by prokaryotic metallothionein. Involvement of Hisimidazole. J. Biol. Chem. 273, 22957–22961 (1998)Search in Google Scholar

[15]Darwin K.H.: Mycobaterium tuberculosis and copper: a newly appreciated defense against an old foe? J. Biol. Chem. 290, 18962–18966 (2015)Search in Google Scholar

[16]Enshaei M., Khanafari A., Sepahey A.A.: Metallothionein induction in two species of Pseudomonas exposed to cadmium and copper contamination. Iran J. Environ. Health Sci. Eng. 7, 287–298 (2010)Search in Google Scholar

[17]Erbe J.L., Taylor K.B., Hall L.M.: Metalloregulation of the cyanobacterial smt locus: identification of SmtB binding sites and direct interaction with metals. Nucl. Acids Res. 23, 2472–2478 (1995)10.1093/nar/23.13.24723070537630724Search in Google Scholar

[18]Festa R.A., Jones M.B., Butler-Wu S., Sinsimer D., Gerads R., Bishai W.R., Peterson S.N., Darwin K.H.: A novel copper-responsive regulon in Mycobacterium tuberculosis. Mol. Microbiol. 79, 133–148 (2011)Search in Google Scholar

[19]Foster A.W., Robinson N.J.: Promiscuity and preferences of metallothioneins: the cell rules. BMC Biol. 9, 25–28 (2011)10.1186/1741-7007-9-25308417821527046Search in Google Scholar

[20]Freisinger E.: Plant MTs – long neglected members of the metallothionein superfamily. Dalton Trans. 47, 6663–6675 (2008)10.1039/b809789e19153613Search in Google Scholar

[21]Godt J., Scheidig F., Grosse-Siestrup C., Esche V., Brandenburg P., Reich A., Gronberg D.A.: The toxicity of cadmium and resulting hazards for human health. J. Occup. Med. Toxicol. 1, 22 (2006)10.1186/1745-6673-1-22157857316961932Search in Google Scholar

[22]Gold B., Deng H., Bryk R., Vargas D., Eliezer D., Roberts J., Jiang X., Nathan C.: Identification of a copper-binding metallothionein in pathogenic mycobacterial. Nat. Chem. Biol. 4, 609–616 (2008)Search in Google Scholar

[23]Gupta A., Whitton B.A., Morby A.P., Huckle J.W., Robinson N.J.: Amplification and rearrangement of a prokaryotic metallothionein locus smt in Synechococcus PCC 6301 selected for tolerance to cadmium. Proc. Biol. Sci. 248, 273–281 (1992)Search in Google Scholar

[24]Hänsch R., Mendel R.R.: Physiological functions of mineral micronutrients (Cu, Zn, Mn, Fe, Ni, Mo, B, Cl). Curr. Opin. Plant Biol. 12, 259–266 (2009)Search in Google Scholar

[25]Higham D.R, Sadler PJ., Scawen M.D.: Cadmium-resistant Pseudomonas putida synthesizes novel cadmium proteins. Science, 225, 1043–1046 (1984)10.1126/science.225.4666.104317783048Search in Google Scholar

[26]Higham D.P., Sadler P.J., Scawen M.D.: Cadmium-binding proteins in Pseudomonas putida: pseudothioneins. Environ. Health Persp. 65, 5–11 (1986)Search in Google Scholar

[27]Higgins K.A., Giedroc D.: Insights into protein allostery in the CsoR/RcnR family of transcriptional repressors. Chem. Lett. 43, 20–25 (2014)Search in Google Scholar

[28]Huckle J.W., Morby A.P., Turner J.S., Robinson N.J.: Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions. Mol. Microbiol. 7, 177–187 (1993)Search in Google Scholar

[29]Koszucka A.M., Dąbrowska G.: Roślinne metalotioneiny. Post. Biol. Kom. 33, 285–302 (2006)Search in Google Scholar

[30]Kuroda M., Hayashi H., Ohta T.: Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912. Microbiol. Immunol. 43, 115–125 (1999)Search in Google Scholar

[31]Lane B., Kajoika R., Kennedy R.: The wheat-germ E_c protein is a zinc-containing metallothionein. Biochem. Cell Biol. 65, 1001–1005 (1987)Search in Google Scholar

[32]Lane T.W., Saito M.A., George G.N., Pickering I.J, Prince R.C., Morel F.M.M.: A cadmium enzyme from a marine diatom. Nature, 435, 42 (2005)10.1038/435042aSearch in Google Scholar

[33]Leszczyszyn O.I., White C.R.J., Blindauer C.A.: The isolated Cys₂His₂ site in E_c metallothionein mediates metal-specific protein folding. Mol. Bio. Syst. 6, 1592–1603 (2010)Search in Google Scholar

[34]Leszczyszyn O.I., Imam H.T., Blindauer C.A.: Diversity and distribution of plant metallothioneins: a review of structure, properties and functions. Metallomics, 5, 1146–1169 (2013)10.1039/c3mt00072aSearch in Google Scholar

[35]Liu T., Nakashima S., Hirose K., Shibasaka M., Katsuhara M., Ezaki B., Giedroc P.D., Kasamo K.: A novel cyanobacterial SmtB/ArsR family repressor regulates the expression of a CPX-ATPase and a metallothionein in response to both Cu(I)/Ag(I) and Zn(II)/Cd(II). J. Biol. Chem. 279, 17810–17818 (2004)Search in Google Scholar

[36]Liu T., Nakashima S., Hirose K., Uemura Y., Shibasaka M., Katsuhara M., Kasamo K.: A metallothionein and CPx-ATPase handle heavy-metal tolerance in the filamentous cyanobacterium Oscillatoria brevis. FEBS Lett. 542, 159–163 (2003)10.1016/S0014-5793(03)00370-3Search in Google Scholar

[37]Ma Z., Jacobsen F.E., Giedroc D.P.: Metal transporters and metal sensors: how coordination chemistry controls bacterial metal homeostasis. Chem. Rev. 109, 4644–4681 (2009)Search in Google Scholar

[38]Maret W., Sandstead H.: Zinc requirements and the risks and benefits of zinc supplementation. J. Trace Elem. Med. Biol. 20, 3–20 (2005)Search in Google Scholar

[39]Margoshes M., Vallee B.L.: A cadmium protein from equine kidney cortex. J. Am. Chem. Soc. 79, 4813–4814 (1957)Search in Google Scholar

[40]Morby A.P., Turner J.S., Huckle J.W., Robinson N.J.: SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucl. Acids Res. 21, 921–925 (1993)10.1093/nar/21.4.921Search in Google Scholar

[41]Naik M.M., Pandey A., Dubey S.K.: Pseudomonas aeruginosa strain WI-1 from Mandovi estuary possesses metallothionein to alleviate lead toxicity and promotes plant growth. Ecotoxicol. Environ. Saf. 79, 129–133 (2012)Search in Google Scholar

[42]Olafson R.W., Abel K., Sim R.G.: Prokaryotic metallothionein: preliminary characterization of a blue-green alga heavy metal-binding protein. Biochem. Biophys. Res. Commun. 89, 36–43 (1979)Search in Google Scholar

[43]Olafson R.W., Loya S., Sim R.G.: Physiological parameters of prokaryotic metallothionein induction. Biochem. Biophys. Res. Commun. 95, 1495–1503 (1980)Search in Google Scholar

[44]Olafson R.W., McCubbin W.D., Kay C.M.: Primary- and secondary-structural analysis of a unique prokaryotic metallothionein from a Synechococcus sp. cyanobacterium. Biochem. J. 251, 691–699 (1988)Search in Google Scholar

[45]Palmer C.M., Guerinot M.L.: Facing the challenges of Cu, Fe and Zn homeostasis in plants. Nat. Chem. Biol. 5, 333–340 (2009)Search in Google Scholar

[46]Pedersen M., Larsen A., Stoltenberg M., Penkova M.: Cell death in the injured brain: Roles of metallothioneins. Prog. Histochem. Cytochem. 44, 1–27 (2009)Search in Google Scholar

[47]Pedersen M., Larsen A., Stoltenberg M., Penkova M.: The role of metallothionein in oncogenesis and cancer prognosis. Prog. Histochem. Cytochem. 44, 29–64 (2009)Search in Google Scholar

[48]Robinson N.J., Tommey A.M., Kuske C., Jackson P.J.: Plant metallothioneins. Biochem. J. 295, 1–10 (1993)Search in Google Scholar

[49]Robinson N.J., Whitehall S.K., Cavet J.S.: Microbial metallothioneins. Adv. Microb. Physiol. 44, 183–213 (2001)Search in Google Scholar

[50]Rowland J.L., Niederweis M.: Resistance mechanism of Mycobacterium tuberculosis against phagosomal copper overload. Tuberculosis, 92, 202–210 (2012)10.1016/j.tube.2011.12.006Search in Google Scholar

[51]Shi J., Lindsay W.P., Huckle J.W., Morby A.P., Robinson N.J.: Cyanobacterial metallothionein gene expressed in Escherichia coli. Metal-binding properties of the expressed protein. FEBS Lett. 2–3, 159–163 (1992)10.1016/0014-5793(92)80509-FSearch in Google Scholar

[52]Shimizu T., Hiyama T., Ikeuchi M., Inoue Y.: Nucleotide sequence of a metallothionein gene of the thermophilic cyanobacterium Synechococcus vulcanus. Plant Mol. Biol. 20, 565–567 (1992)Search in Google Scholar

[53]Silver S., Phung L.T.: Bacterial heavy metal resistance: new surprises. Annu. Rev. Microbiol. 50, 753–789 (1996)10.1146/annurev.micro.50.1.7538905098Search in Google Scholar

[54]Stępkowska I.M.: Właściwości biologiczne metalotionein i ich udział w procesach oksydoredukcyjnych w komórkach, ze szczególnym uwzględnieniem ośrodkowego układu nerwowego człowieka. Post. Biol. Kom. 37, 869–885 (2010)Search in Google Scholar

[55]Sutherland D.E., Stillman M.J.: The “magic numbers” of metallothionein. Metallomics, 3, 444–463 (2011)10.1039/c0mt00102c21409206Search in Google Scholar

[56]Thelwell C., Robinson N.J., Turner-Cavet J.S.: An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter. Proc. Natl. Acad. Sci. USA, 95, 10728–10733 (1998)10.1073/pnas.95.18.10728279639724772Search in Google Scholar

[57]Turner J.S., Glands P.D., Samson A.C.R., Robinson N.J.: Zn²⁺-Sensing by the cyanobacterial metallothionein repressor SmtB: different motifs mediate metal-induced protein-DNA dissociation. Nucl. Acids Res. 24, 3714–3721 (1996)10.1093/nar/24.19.37141461718871549Search in Google Scholar

[58]Turner J.S., Morby A.P., Whitton B.A., Gupta A., Robinson N.J.: Construction and characterisation of Zn²⁺/Cd²⁺ hypersensitive cyanobacterial mutants lacking a functional metallothionein locus. J. Biol. Chem. 268, 4494–4498 (1993)Search in Google Scholar

[59]Vašák M.: Advances in metallothionein structure and functions. J. Trace Elem. Med. Biol. 19, 13–17 (2005)Search in Google Scholar

[60]Waldron K.J., Robinson N.J.: How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol. 7, 25–35 (2009)Search in Google Scholar