Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv
Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv073...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Zhang, Xuelian [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2009 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media, LLC 2009 |
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| Übergeordnetes Werk: |
Enthalten in: Current microbiology - New York, NY : Springer, 1978, 59(2009), 5 vom: 18. Aug. |
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| Übergeordnetes Werk: |
volume:59 ; year:2009 ; number:5 ; day:18 ; month:08 |
| Links: |
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| DOI / URN: |
10.1007/s00284-009-9470-3 |
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| Katalog-ID: |
SPR003669831 |
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| 100 | 1 | |a Zhang, Xuelian |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv |
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| 520 | |a Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. | ||
| 650 | 4 | |a Tuberculosis |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Tuberculosis H37Rv |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Stationary Phase Culture |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Rv0734 Gene |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Mycobacterium Tuberculosis H37Rv |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Chen, Shudan |4 aut | |
| 700 | 1 | |a Hu, Zhidong |4 aut | |
| 700 | 1 | |a Zhang, Lu |4 aut | |
| 700 | 1 | |a Wang, Honghai |4 aut | |
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10.1007/s00284-009-9470-3 doi (DE-627)SPR003669831 (SPR)s00284-009-9470-3-e DE-627 ger DE-627 rakwb eng Zhang, Xuelian verfasserin aut Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2009 Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. Tuberculosis (dpeaa)DE-He213 Tuberculosis H37Rv (dpeaa)DE-He213 Stationary Phase Culture (dpeaa)DE-He213 Rv0734 Gene (dpeaa)DE-He213 Mycobacterium Tuberculosis H37Rv (dpeaa)DE-He213 Chen, Shudan aut Hu, Zhidong aut Zhang, Lu aut Wang, Honghai aut Enthalten in Current microbiology New York, NY : Springer, 1978 59(2009), 5 vom: 18. Aug. (DE-627)253722160 (DE-600)1458987-4 1432-0991 nnns volume:59 year:2009 number:5 day:18 month:08 https://dx.doi.org/10.1007/s00284-009-9470-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 59 2009 5 18 08 |
| spelling |
10.1007/s00284-009-9470-3 doi (DE-627)SPR003669831 (SPR)s00284-009-9470-3-e DE-627 ger DE-627 rakwb eng Zhang, Xuelian verfasserin aut Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2009 Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. Tuberculosis (dpeaa)DE-He213 Tuberculosis H37Rv (dpeaa)DE-He213 Stationary Phase Culture (dpeaa)DE-He213 Rv0734 Gene (dpeaa)DE-He213 Mycobacterium Tuberculosis H37Rv (dpeaa)DE-He213 Chen, Shudan aut Hu, Zhidong aut Zhang, Lu aut Wang, Honghai aut Enthalten in Current microbiology New York, NY : Springer, 1978 59(2009), 5 vom: 18. Aug. (DE-627)253722160 (DE-600)1458987-4 1432-0991 nnns volume:59 year:2009 number:5 day:18 month:08 https://dx.doi.org/10.1007/s00284-009-9470-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 59 2009 5 18 08 |
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10.1007/s00284-009-9470-3 doi (DE-627)SPR003669831 (SPR)s00284-009-9470-3-e DE-627 ger DE-627 rakwb eng Zhang, Xuelian verfasserin aut Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2009 Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. Tuberculosis (dpeaa)DE-He213 Tuberculosis H37Rv (dpeaa)DE-He213 Stationary Phase Culture (dpeaa)DE-He213 Rv0734 Gene (dpeaa)DE-He213 Mycobacterium Tuberculosis H37Rv (dpeaa)DE-He213 Chen, Shudan aut Hu, Zhidong aut Zhang, Lu aut Wang, Honghai aut Enthalten in Current microbiology New York, NY : Springer, 1978 59(2009), 5 vom: 18. Aug. (DE-627)253722160 (DE-600)1458987-4 1432-0991 nnns volume:59 year:2009 number:5 day:18 month:08 https://dx.doi.org/10.1007/s00284-009-9470-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 59 2009 5 18 08 |
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10.1007/s00284-009-9470-3 doi (DE-627)SPR003669831 (SPR)s00284-009-9470-3-e DE-627 ger DE-627 rakwb eng Zhang, Xuelian verfasserin aut Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2009 Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. Tuberculosis (dpeaa)DE-He213 Tuberculosis H37Rv (dpeaa)DE-He213 Stationary Phase Culture (dpeaa)DE-He213 Rv0734 Gene (dpeaa)DE-He213 Mycobacterium Tuberculosis H37Rv (dpeaa)DE-He213 Chen, Shudan aut Hu, Zhidong aut Zhang, Lu aut Wang, Honghai aut Enthalten in Current microbiology New York, NY : Springer, 1978 59(2009), 5 vom: 18. Aug. (DE-627)253722160 (DE-600)1458987-4 1432-0991 nnns volume:59 year:2009 number:5 day:18 month:08 https://dx.doi.org/10.1007/s00284-009-9470-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 59 2009 5 18 08 |
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10.1007/s00284-009-9470-3 doi (DE-627)SPR003669831 (SPR)s00284-009-9470-3-e DE-627 ger DE-627 rakwb eng Zhang, Xuelian verfasserin aut Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2009 Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. Tuberculosis (dpeaa)DE-He213 Tuberculosis H37Rv (dpeaa)DE-He213 Stationary Phase Culture (dpeaa)DE-He213 Rv0734 Gene (dpeaa)DE-He213 Mycobacterium Tuberculosis H37Rv (dpeaa)DE-He213 Chen, Shudan aut Hu, Zhidong aut Zhang, Lu aut Wang, Honghai aut Enthalten in Current microbiology New York, NY : Springer, 1978 59(2009), 5 vom: 18. Aug. (DE-627)253722160 (DE-600)1458987-4 1432-0991 nnns volume:59 year:2009 number:5 day:18 month:08 https://dx.doi.org/10.1007/s00284-009-9470-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 59 2009 5 18 08 |
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Enthalten in Current microbiology 59(2009), 5 vom: 18. Aug. volume:59 year:2009 number:5 day:18 month:08 |
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Zhang, Xuelian @@aut@@ Chen, Shudan @@aut@@ Hu, Zhidong @@aut@@ Zhang, Lu @@aut@@ Wang, Honghai @@aut@@ |
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To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. 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|
| author |
Zhang, Xuelian |
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Zhang, Xuelian misc Tuberculosis misc Tuberculosis H37Rv misc Stationary Phase Culture misc Rv0734 Gene misc Mycobacterium Tuberculosis H37Rv Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv |
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Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv Tuberculosis (dpeaa)DE-He213 Tuberculosis H37Rv (dpeaa)DE-He213 Stationary Phase Culture (dpeaa)DE-He213 Rv0734 Gene (dpeaa)DE-He213 Mycobacterium Tuberculosis H37Rv (dpeaa)DE-He213 |
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misc Tuberculosis misc Tuberculosis H37Rv misc Stationary Phase Culture misc Rv0734 Gene misc Mycobacterium Tuberculosis H37Rv |
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misc Tuberculosis misc Tuberculosis H37Rv misc Stationary Phase Culture misc Rv0734 Gene misc Mycobacterium Tuberculosis H37Rv |
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Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv |
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Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv |
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Zhang, Xuelian |
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Current microbiology |
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Zhang, Xuelian Chen, Shudan Hu, Zhidong Zhang, Lu Wang, Honghai |
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Zhang, Xuelian |
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10.1007/s00284-009-9470-3 |
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expression and characterization of two functional methionine aminopeptidases from mycobacterium tuberculosis h37rv |
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Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv |
| abstract |
Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. © Springer Science+Business Media, LLC 2009 |
| abstractGer |
Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. © Springer Science+Business Media, LLC 2009 |
| abstract_unstemmed |
Abstract Methionine aminopeptidase (MetAP) carries out an essential posttranslational modification of nascent proteins by removing the N-terminal methionine and is a potential target for discovering antibacterial agents. To characterize and compare the two MetAPs in Mycobacterium tuberculosis, Rv0734 and Rv2861c genes encoding MetAPs from genome of Mycobacterium tuberculosis H37Rv were cloned and expressed in Escherichia coli. Comparative analysis showed that the two recombinant Mycobacterium tuberculosis MetAPs (MtMetAPs, with 6His-tag being cleaved) have different activities in their substrate specificity, divalent ion requirement, and temperature optima. The temperature for MtMetAP1a and MtMetAP1c were 55 and 37°C, respectively, and MtMetAP1a was found to have good temperature stability. The activities of MtMetAPs were increased by $ Co^{2+} $ ions, but were strongly inhibited by $ Cu^{2+} $, $ Fe^{2+} $, and $ Ni^{2+} $. In addition, the MtMetAP1a and MtMetAP1c activities were stimulated by $ Mg^{2+} $ and $ Zn^{2+} $, respectively. Transcriptional comparative analysis of these two genes revealed that, in both H37Ra and H37Rv, there was approximately a 2-fold decrease of Rv0734 transcripts in 60-day-old stationary phase culture comparing to that in 14-day-old log phase bacilli. On the other hand, the transcription level of Rv2861c in tested mycobacteria in log phase culture was nearly 1.5 times lower than that in stationary phase culture. The result suggests that the two MtMetMAPs may perform important function in different growth phases of Mycobacterium tuberculosis. © Springer Science+Business Media, LLC 2009 |
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| title_short |
Expression and Characterization of Two Functional Methionine Aminopeptidases from Mycobacterium tuberculosis H37Rv |
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https://dx.doi.org/10.1007/s00284-009-9470-3 |
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Chen, Shudan Hu, Zhidong Zhang, Lu Wang, Honghai |
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| doi_str |
10.1007/s00284-009-9470-3 |
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2024-07-03T20:54:32.250Z |
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| score |
7.3987417 |