Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen
Haem-dependent catalase is an antioxidant enzyme that degrades H2O2, producing H2O and O2, and is common in aerobes. Catalase is present in some strictly anaerobic methane-producing archaea (methanogens), but the importance of catalase to the antioxidant system of methanogens is poorly understood. W...
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Published in | Microbiology (Society for General Microbiology) Vol. 160; no. Pt 2; pp. 270 - 278 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
Society for General Microbiology
01.02.2014
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Abstract | Haem-dependent catalase is an antioxidant enzyme that degrades H2O2, producing H2O and O2, and is common in aerobes. Catalase is present in some strictly anaerobic methane-producing archaea (methanogens), but the importance of catalase to the antioxidant system of methanogens is poorly understood. We report here that a survey of the sequenced genomes of methanogens revealed that the majority of species lack genes encoding catalase. Moreover, Methanosarcina acetivorans is a methanogen capable of synthesizing haem and encodes haem-dependent catalase in its genome; yet, Methanosarcina acetivorans cells lack detectable catalase activity. However, inducible expression of the haem-dependent catalase from Escherichia coli (EcKatG) in the chromosome of Methanosarcina acetivorans resulted in a 100-fold increase in the endogenous catalase activity compared with uninduced cells. The increased catalase activity conferred a 10-fold increase in the resistance of EcKatG-induced cells to H2O2 compared with uninduced cells. The EcKatG-induced cells were also able to grow when exposed to levels of H2O2 that inhibited or killed uninduced cells. However, despite the significant increase in catalase activity, growth studies revealed that EcKatG-induced cells did not exhibit increased tolerance to O2 compared with uninduced cells. These results support the lack of catalase in the majority of methanogens, since methanogens are more likely to encounter O2 rather than high concentrations of H2O2 in the natural environment. Catalase appears to be a minor component of the antioxidant system in methanogens, even those that are aerotolerant, including Methanosarcina acetivorans. Importantly, the experimental approach used here demonstrated the feasibility of engineering beneficial traits, such as H2O2 tolerance, in methanogens. |
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AbstractList | Haem-dependent catalase is an antioxidant enzyme that degrades H
2
O
2
, producing H
2
O and O
2
, and is common in aerobes. Catalase is present in some strictly anaerobic methane-producing archaea (methanogens), but the importance of catalase to the antioxidant system of methanogens is poorly understood. We report here that a survey of the sequenced genomes of methanogens revealed that the majority of species lack genes encoding catalase. Moreover,
Methanosarcina acetivorans
is a methanogen capable of synthesizing haem and encodes haem-dependent catalase in its genome; yet,
Methanosarcina acetivorans
cells lack detectable catalase activity. However, inducible expression of the haem-dependent catalase from
Escherichia coli
(EcKatG) in the chromosome of
Methanosarcina acetivorans
resulted in a 100-fold increase in the endogenous catalase activity compared with uninduced cells. The increased catalase activity conferred a 10-fold increase in the resistance of EcKatG-induced cells to H
2
O
2
compared with uninduced cells. The EcKatG-induced cells were also able to grow when exposed to levels of H
2
O
2
that inhibited or killed uninduced cells. However, despite the significant increase in catalase activity, growth studies revealed that EcKatG-induced cells did not exhibit increased tolerance to O
2
compared with uninduced cells. These results support the lack of catalase in the majority of methanogens, since methanogens are more likely to encounter O
2
rather than high concentrations of H
2
O
2
in the natural environment. Catalase appears to be a minor component of the antioxidant system in methanogens, even those that are aerotolerant, including
Methanosarcina acetivorans
. Importantly, the experimental approach used here demonstrated the feasibility of engineering beneficial traits, such as H
2
O
2
tolerance, in methanogens. Haem-dependent catalase is an antioxidant enzyme that degrades H2O2, producing H2O and O2, and is common in aerobes. Catalase is present in some strictly anaerobic methane-producing archaea (methanogens), but the importance of catalase to the antioxidant system of methanogens is poorly understood. We report here that a survey of the sequenced genomes of methanogens revealed that the majority of species lack genes encoding catalase. Moreover, Methanosarcina acetivorans is a methanogen capable of synthesizing haem and encodes haem-dependent catalase in its genome; yet, Methanosarcina acetivorans cells lack detectable catalase activity. However, inducible expression of the haem-dependent catalase from Escherichia coli (EcKatG) in the chromosome of Methanosarcina acetivorans resulted in a 100-fold increase in the endogenous catalase activity compared with uninduced cells. The increased catalase activity conferred a 10-fold increase in the resistance of EcKatG-induced cells to H2O2 compared with uninduced cells. The EcKatG-induced cells were also able to grow when exposed to levels of H2O2 that inhibited or killed uninduced cells. However, despite the significant increase in catalase activity, growth studies revealed that EcKatG-induced cells did not exhibit increased tolerance to O2 compared with uninduced cells. These results support the lack of catalase in the majority of methanogens, since methanogens are more likely to encounter O2 rather than high concentrations of H2O2 in the natural environment. Catalase appears to be a minor component of the antioxidant system in methanogens, even those that are aerotolerant, including Methanosarcina acetivorans. Importantly, the experimental approach used here demonstrated the feasibility of engineering beneficial traits, such as H2O2 tolerance, in methanogens. |
Author | Jennings, Matthew E Lessner, Daniel J Horne, Alexandra J Schaff, Cody W Lessner, Faith H |
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References | r2 r3 r4 r5 r6 r7 r9 r30 r10 r31 r12 r11 r14 r13 r16 r15 r18 r17 r19 Colt (r8) 1984 Lessner (r20) 2010; 1 Sowers (r27) 1984; 47 r21 r23 r22 r25 r24 r26 r29 r28 r1 |
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Snippet | Haem-dependent catalase is an antioxidant enzyme that degrades H2O2, producing H2O and O2, and is common in aerobes. Catalase is present in some strictly... Haem-dependent catalase is an antioxidant enzyme that degrades H 2 O 2 , producing H 2 O and O 2 , and is common in aerobes. Catalase is present in some... |
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SubjectTerms | Catalase - biosynthesis Catalase - genetics Cell and Molecular Biology of Microbes Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - biosynthesis Escherichia coli Proteins - genetics Gene Expression Hydrogen Peroxide - metabolism Hydrogen Peroxide - toxicity Methanosarcina - drug effects Methanosarcina - enzymology Methanosarcina - genetics Methanosarcina - metabolism Microbial Viability - drug effects Oxygen - metabolism Oxygen - toxicity Recombinant Proteins - biosynthesis Recombinant Proteins - genetics |
Title | Expression of a bacterial catalase in a strictly anaerobic methanogen significantly increases tolerance to hydrogen peroxide but not oxygen |
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