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1

Peña, Carol E. A., J. Michelle Kahlenberg, and Graham F. Hatfull. "Protein-DNA Complexes in Mycobacteriophage L5 Integrative Recombination." Journal of Bacteriology 181, no. 2 (1999): 454–61. http://dx.doi.org/10.1128/jb.181.2.454-461.1999.

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ABSTRACT The temperate mycobacteriophage L5 integrates site specifically into the genomes of Mycobacterium smegmatis,Mycobacterium tuberculosis, and Mycobacterium bovis bacillus Calmette-Guérin. This integrative recombination event occurs between the phage L5 attP site and the mycobacterial attB site and requires the phage-encoded integrase and mycobacterial-encoded integration host factor mIHF. Here we show that attP, Int-L5, and mIHF assemble into a recombinationally active complex, the intasome, which is capable of attB capture and formation of products. The arm-type integrase binding site
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2

Singhal, Anshika, Richa Virmani, Saba Naz, et al. "Methylation of two-component response regulator MtrA in mycobacteria negatively modulates its DNA binding and transcriptional activation." Biochemical Journal 477, no. 23 (2020): 4473–89. http://dx.doi.org/10.1042/bcj20200455.

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Post-translational modifications such as phosphorylation, nitrosylation, and pupylation modulate multiple cellular processes in Mycobacterium tuberculosis. While protein methylation at lysine and arginine residues is widespread in eukaryotes, to date only two methylated proteins in Mtb have been identified. Here, we report the identification of methylation at lysine and/or arginine residues in nine mycobacterial proteins. Among the proteins identified, we chose MtrA, an essential response regulator of a two-component signaling system, which gets methylated on multiple lysine and arginine resid
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3

Bai, Guangchun, Michaela A. Gazdik, Damen D. Schaak, and Kathleen A. McDonough. "The Mycobacterium bovis BCG Cyclic AMP Receptor-Like Protein Is a Functional DNA Binding Protein In Vitro and In Vivo, but Its Activity Differs from That of Its M. tuberculosis Ortholog, Rv3676." Infection and Immunity 75, no. 11 (2007): 5509–17. http://dx.doi.org/10.1128/iai.00658-07.

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ABSTRACT Mycobacterium tuberculosis Rv3676 encodes a cyclic AMP (cAMP) receptor-like protein (CRPMt) that has been implicated in global gene regulation and may play an important role during tuberculosis infection. The CRPMt ortholog in Mycobacterium bovis BCG, CRPBCG, is dysfunctional in an Escherichia coli CRP competition assay and has been proposed as a potential source of M. bovis BCG's attenuation. We compared CRPBCG and CRPMt in vitro and in vivo, in M. bovis BCG and M. tuberculosis, to evaluate CRPBCG's potential function in a mycobacterial system. Both proteins formed dimers in mycobact
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4

Gigante, Adriano M., Francisco Olivença, Maria João Catalão, et al. "The Mycobacteriophage Ms6 LysB N-Terminus Displays Peptidoglycan Binding Affinity." Viruses 13, no. 7 (2021): 1377. http://dx.doi.org/10.3390/v13071377.

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Double-stranded DNA bacteriophages end their lytic cycle by disrupting the host cell envelope, which allows the release of the virion progeny. Each phage must synthesize lysis proteins that target each cell barrier to phage release. In addition to holins, which permeabilize the cytoplasmic membrane, and endolysins, which disrupt the peptidoglycan (PG), mycobacteriophages synthesize a specific lysis protein, LysB, capable of detaching the outer membrane from the complex cell wall of mycobacteria. The family of LysB proteins is highly diverse, with many members presenting an extended N-terminus.
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5

Spreadbury, Claire L., Mark J. Pallen, Tim Overton, et al. "Point mutations in the DNA- and cNMP-binding domains of the homologue of the cAMP receptor protein (CRP) in Mycobacterium bovis BCG: implications for the inactivation of a global regulator and strain attenuation." Microbiology 151, no. 2 (2005): 547–56. http://dx.doi.org/10.1099/mic.0.27444-0.

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The genome of Mycobacterium tuberculosis H37Rv includes a homologue of the CRP/FNR (cAMP receptor protein/fumarate and nitrate reduction regulator) family of transcription regulators encoded by Rv3676. Sequencing of the orthologous gene from attenuated Mycobacterium bovis Bacille Calmette–Guérin (BCG) strains revealed point mutations that affect the putative DNA-binding and cNMP-binding domains of the encoded protein. These mutations are not present in the published sequences of the Rv3676 orthologues in M. bovis, M. tuberculosis or Mycobacterium leprae. An Escherichia coli lacZ reporter syst
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6

ZAWILAK, Anna, Agnieszka KOIS, Grażyna KONOPA, Aleksandra SMULCZYK-KRAWCZYSZYN, and Jolanta ZAKRZEWSKA-CZERWIŃSKA. "Mycobacterium tuberculosis DnaA initiator protein: purification and DNA-binding requirements." Biochemical Journal 382, no. 1 (2004): 247–52. http://dx.doi.org/10.1042/bj20040338.

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The Mycobacterium tuberculosis oriC (the origin of chromosomal replication) region contains 13 non-perfect DnaA boxes. The M. tuberculosis initiator protein, DnaA, was overexpressed in Escherichia coli as a soluble His-tagged fusion protein. The purified protein His6MtDnaA was investigated for its binding properties to DnaA boxes from the oriC region. Gel retardation demonstrated that the DnaA from M. tuberculosis requires two DnaA boxes for efficient binding. Electron microscopy as well as DNase I footprinting showed that the His6MtDnaA protein binds to four specific regions, which correspond
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7

Sala, Claudia, Francesca Forti, Elisabetta Di Florio, et al. "Mycobacterium tuberculosis FurA Autoregulates Its Own Expression." Journal of Bacteriology 185, no. 18 (2003): 5357–62. http://dx.doi.org/10.1128/jb.185.18.5357-5362.2003.

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ABSTRACT The furA-katG region of Mycobacterium tuberculosis, encoding a Fur-like protein and the catalase-peroxidase, is highly conserved among mycobacteria. Both genes are induced upon oxidative stress. In this work we analyzed the M. tuberculosis furA promoter region. DNA fragments were cloned upstream of the luciferase reporter gene, and promoter activity in Mycobacterium smegmatis was measured in both the presence and absence of oxidative stress. The shortest fragment containing an inducible promoter extends 45 bp upstream of furA. In this region, −35 and −10 promoter consensus sequences c
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8

Bai, Guangchun, Lee Ann McCue, and Kathleen A. McDonough. "Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a Cyclic AMP Receptor Protein-Like DNA Binding Protein." Journal of Bacteriology 187, no. 22 (2005): 7795–804. http://dx.doi.org/10.1128/jb.187.22.7795-7804.2005.

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ABSTRACT Little is known about cyclic AMP (cAMP) function in Mycobacterium tuberculosis, despite its ability to encode 15 adenylate cyclases and 10 cNMP-binding proteins. M. tuberculosis Rv3676, which we have designated CRPMt, is predicted to be a cAMP-dependent transcription factor. In this study, we characterized CRPMt's interactions with DNA and cAMP, using experimental and computational approaches. We used Gibbs sampling to define a CRPMt DNA motif that resembles the cAMP receptor protein (CRP) binding motif model for Escherichia coli. CRPMt binding sites were identified in a total of 73 p
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9

Miggiano, Riccardo, Giuseppe Perugino, Maria Ciaramella, et al. "Crystal structure of Mycobacterium tuberculosis O6-methylguanine-DNA methyltransferase protein clusters assembled on to damaged DNA." Biochemical Journal 473, no. 2 (2016): 123–33. http://dx.doi.org/10.1042/bj20150833.

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Mycobacterium tuberculosis directly repairs alkylated bases in DNA through the action of OGT. We reveal new molecular details of damaged-DNA recognition and co-operative binding by MtOGT, highlighting the peculiar structural flexibility of the protein.
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10

Mishra, Alok K., Shivraj M. Yabaji, Rikesh K. Dubey, Ekta Dhamija, and Kishore K. Srivastava. "Dual phosphorylation in response regulator protein PrrA is crucial for intracellular survival of mycobacteria consequent upon transcriptional activation." Biochemical Journal 474, no. 24 (2017): 4119–36. http://dx.doi.org/10.1042/bcj20170596.

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The remarkable ability of Mycobacterium tuberculosis (Mtb) to survive inside human macrophages is attributed to the presence of a complex sensory and regulatory network. PrrA is a DNA-binding regulatory protein, belonging to an essential two-component system (TCS), PrrA/B, which is required for early phase intracellular replication of Mtb. Despite its importance, the mechanism of PrrA/B-mediated signaling is not well understood. In the present study, we demonstrate that the binding of PrrA on the promoter DNA and its consequent activation is cumulatively controlled via dual phosphorylation of
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11

Werlang, Isabel C. R., Cristopher Z. Schneider, Jordana D. Mendonça, Mario S. Palma, Luiz A. Basso, and Diógenes S. Santos. "Identification of Rv3852 as a nucleoid-associated protein in Mycobacterium tuberculosis." Microbiology 155, no. 8 (2009): 2652–63. http://dx.doi.org/10.1099/mic.0.030148-0.

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Tuberculosis remains the major cause of mortality due to a bacterial pathogen, Mycobacterium tuberculosis. The molecular mechanisms of infection and persistence have not been completely elucidated for this pathogen. Studies involving nucleoid-associated proteins (NAPs), which have been related to the control and influence of virulence genes in pathogenic bacteria, can help unveil the virulence process of M. tuberculosis. Here, we describe the initial characterization of an ORF for an M. tuberculosis putative NAP. The Rv3852 gene was cloned and expressed, and its product purified to homogeneity
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12

Henderson, Sara R., Clare E. M. Stevenson, Brandon Malone, et al. "Structural and mechanistic analysis of ATPase inhibitors targeting mycobacterial DNA gyrase." Journal of Antimicrobial Chemotherapy 75, no. 10 (2020): 2835–42. http://dx.doi.org/10.1093/jac/dkaa286.

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Abstract Objectives To evaluate the efficacy of two novel compounds against mycobacteria and determine the molecular basis of their action on DNA gyrase using structural and mechanistic approaches. Methods Redx03863 and Redx04739 were tested in antibacterial assays, and also against their target, DNA gyrase, using DNA supercoiling and ATPase assays. X-ray crystallography was used to determine the structure of the gyrase B protein ATPase sub-domain from Mycobacterium smegmatis complexed with the aminocoumarin drug novobiocin, and structures of the same domain from Mycobacterium thermoresistibil
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13

Lewin, Astrid, Daniela Baus, Elisabeth Kamal, et al. "The mycobacterial DNA-binding protein 1 (MDP1) from Mycobacterium bovis BCG influences various growth characteristics." BMC Microbiology 8, no. 1 (2008): 91. http://dx.doi.org/10.1186/1471-2180-8-91.

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14

Nguyen, Kiet T., Kristina Piastro, and Keith M. Derbyshire. "LpqM, a Mycobacterial Lipoprotein-Metalloproteinase, Is Required for Conjugal DNA Transfer in Mycobacterium smegmatis." Journal of Bacteriology 191, no. 8 (2009): 2721–27. http://dx.doi.org/10.1128/jb.00024-09.

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ABSTRACT We have previously described a novel conjugal DNA transfer process that occurs in Mycobacterium smegmatis. To identify donor genes required for transfer, we have performed a transposon mutagenesis screen; we report here that LpqM, a putative lipoprotein-metalloproteinase, is essential for efficient DNA transfer. Bioinformatic analyses predict that LpqM contains a signal peptide necessary for the protein's targeting to the cell envelope and a metal ion binding motif, the likely catalytic site for protease activity. Using targeted mutagenesis, we demonstrate that each of these motifs is
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15

Ganguly, Abantika, Priya Rajdev, Sunanda Margrett Williams, and Dipankar Chatterji. "Nonspecific Interaction between DNA and Protein allows for Cooperativity: A Case Study with Mycobacterium DNA Binding Protein." Journal of Physical Chemistry B 116, no. 1 (2011): 621–32. http://dx.doi.org/10.1021/jp209423n.

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16

Sharma, Kirti, Meetu Gupta, Monika Pathak, et al. "Transcriptional Control of the Mycobacterial embCAB Operon by PknH through a Regulatory Protein, EmbR, In Vivo." Journal of Bacteriology 188, no. 8 (2006): 2936–44. http://dx.doi.org/10.1128/jb.188.8.2936-2944.2006.

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ABSTRACT EmbR, a putative transcriptional regulator from Mycobacterium tuberculosis, is homologous to the OmpR class of transcriptional regulators that possess winged helix-turn-helix DNA binding motifs. In contrast to other OmpR-like response regulators that are usually phosphorylated and controlled by histidine kinases, EmbR was recently shown to be phosphorylated by the cognate mycobacterial serine/threonine kinase PknH. Despite the in vitro evidence of phosphorylation and interaction between the kinase and regulator, the physiological function of the PknH-EmbR pair is still unknown. We ide
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17

Tanghe, Audrey, Philippe Lefèvre, Olivier Denis, et al. "Immunogenicity and Protective Efficacy of Tuberculosis DNA Vaccines Encoding Putative Phosphate Transport Receptors." Journal of Immunology 162, no. 2 (1999): 1113–19. http://dx.doi.org/10.4049/jimmunol.162.2.1113.

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Abstract Using culture filtrate Ag-specific mAbs generated from mycobacteria-infected H-2b haplotype mice, we have previously identified three genes in the Mycobacterium tuberculosis genome, encoding proteins homologous to the periplasmic ATP-binding cassette phosphate-binding receptor PstS of the phosphate-specific transport system of E. coli. To define the potential vaccinal properties of these phosphate-binding proteins, female C57BL/6 mice were injected i.m. with plasmid DNA encoding PstS-1, PstS-2, or PstS-3 proteins from M. tuberculosis and immunogenicity and protective efficacy against
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18

Sinha, Akesh, Sankalp Gupta, Shweta Bhutani, Anuj Pathak, and Dibyendu Sarkar. "PhoP-PhoP Interaction at Adjacent PhoP Binding Sites Is Influenced by Protein Phosphorylation." Journal of Bacteriology 190, no. 4 (2007): 1317–28. http://dx.doi.org/10.1128/jb.01074-07.

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ABSTRACT Mycobacterium tuberculosis PhoP regulates the expression of unknown virulence determinants and the biosynthesis of complex lipids. PhoP, like other members of the OmpR family, comprises a phosphorylation domain at the amino-terminal half and a DNA-binding domain at the carboxy-terminal half of the protein. To explore structural effect of protein phosphorylation and to examine effect of phosphorylation on DNA binding, purified PhoP was phosphorylated by acetyl phosphate in a reaction that was dependent on Mg2+ and Asp-71. Protein phosphorylation was not required for DNA binding; howeve
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19

Gupta, Sankalp, Anuj Pathak, Akesh Sinha, and Dibyendu Sarkar. "Mycobacterium tuberculosis PhoP Recognizes Two Adjacent Direct-Repeat Sequences To Form Head-to-Head Dimers." Journal of Bacteriology 191, no. 24 (2009): 7466–76. http://dx.doi.org/10.1128/jb.00669-09.

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ABSTRACT Mycobacterium tuberculosis PhoP of the PhoP-PhoR two-component signaling system orchestrates a complex transcription program and is essential for the growth and virulence of the tubercle bacillus. PhoP comprises a phosphorylation domain at the amino-terminal half and a DNA-binding domain in the carboxy-terminal half of the protein. We show here that the protein recognizes a 23-bp sequence of the phoP upstream region comprising two adjacent direct repeat motifs believed to promote transcription regulation. DNA binding, which involves the recruitment of two monomeric PhoP molecules, was
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20

Singh, Amandeep, Umesh Varshney, and M. Vijayan. "Structure of the second Single Stranded DNA Binding protein (SSBb) from Mycobacterium smegmatis." Journal of Structural Biology 196, no. 3 (2016): 448–54. http://dx.doi.org/10.1016/j.jsb.2016.09.012.

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21

Smith, Laura J., Melanie R. Stapleton, Gavin J. M. Fullstone, et al. "Mycobacterium tuberculosis WhiB1 is an essential DNA-binding protein with a nitric oxide-sensitive iron–sulfur cluster." Biochemical Journal 432, no. 3 (2010): 417–27. http://dx.doi.org/10.1042/bj20101440.

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Mycobacterium tuberculosis is a major pathogen that has the ability to establish, and emerge from, a persistent state. Wbl family proteins are associated with developmental processes in actinomycetes, and M. tuberculosis has seven such proteins. In the present study it is shown that the M. tuberculosis H37Rv whiB1 gene is essential. The WhiB1 protein possesses a [4Fe-4S]2+ cluster that is stable in air but reacts rapidly with eight equivalents of nitric oxide to yield two dinuclear dinitrosyl-iron thiol complexes. The [4Fe-4S] form of WhiB1 did not bind whiB1 promoter DNA, but the reduced and
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22

Hunt, Debbie M., José W. Saldanha, John F. Brennan, et al. "Single Nucleotide Polymorphisms That Cause Structural Changes in the Cyclic AMP Receptor Protein Transcriptional Regulator of the Tuberculosis Vaccine Strain Mycobacterium bovis BCG Alter Global Gene Expression without Attenuating Growth." Infection and Immunity 76, no. 5 (2008): 2227–34. http://dx.doi.org/10.1128/iai.01410-07.

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ABSTRACT Single nucleotide polymorphisms (SNPs) are present in the global transcriptional regulator cyclic AMP (cAMP) receptor protein (CRP) of the attenuated vaccine strain Mycobacterium bovis, bacillus Calmette-Guérin (BCG). We have found that these SNPs resulted in small but significant changes in the expression of a number of genes in M. tuberculosis when a deletion of the Rv3676 CRP was complemented by the BCG allele, compared to complementation by the M. tuberculosis allele. We can explain these changes in gene expression by modeling the structure of the mycobacterial protein on the kno
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23

Nguyen, Kiet T., Kristina Piastro, Todd A. Gray, and Keith M. Derbyshire. "Mycobacterial Biofilms Facilitate Horizontal DNA Transfer between Strains of Mycobacterium smegmatis." Journal of Bacteriology 192, no. 19 (2010): 5134–42. http://dx.doi.org/10.1128/jb.00650-10.

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ABSTRACT Conjugal transfer of chromosomal DNA between strains of Mycobacterium smegmatis occurs by a novel mechanism. In a transposon mutagenesis screen, three transfer-defective insertions were mapped to the lsr2 gene of the donor strain mc2155. Because lsr2 encodes a nonspecific DNA-binding protein, mutations of lsr2 give rise to a variety of phenotypes, including an inability to form biofilms. In this study, we show that efficient DNA transfer between strains of M. smegmatis occurs in a mixed biofilm and that the process requires expression of lsr2 in the donor but not in the recipient stra
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24

Dubnau, Eugenie, Patricia Fontán, Riccardo Manganelli, Sonia Soares-Appel, and Issar Smith. "Mycobacterium tuberculosis Genes Induced during Infection of Human Macrophages." Infection and Immunity 70, no. 6 (2002): 2787–95. http://dx.doi.org/10.1128/iai.70.6.2787-2795.2002.

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ABSTRACT We identified Mycobacterium tuberculosis genes preferentially expressed during infection of human macrophages using a promoter trap adapted for this pathogen. inhA encodes an enoyl-acyl carrier protein reductase that is required for mycolic acid biosynthesis (A. Quemard et al., Biochemistry 34:8235-8241, 1995) and is a major target for isoniazid (INH) in mycobacterial species (A. Banerjee et al., Science 263:227-230, 1994). Since overexpression of inhA confers INH resistance in Mycobacterium smegmatis (Banerjee et al., Science 263:227-230, 1994), we designed a promoter trap based on t
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Brooks, Patricia C., Farahnaz Movahedzadeh, and Elaine O. Davis. "Identification of Some DNA Damage-Inducible Genes of Mycobacterium tuberculosis: Apparent Lack of Correlation with LexA Binding." Journal of Bacteriology 183, no. 15 (2001): 4459–67. http://dx.doi.org/10.1128/jb.183.15.4459-4467.2001.

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ABSTRACT The repair of DNA damage is expected to be particularly important to intracellular pathogens such as Mycobacterium tuberculosis, and so it is of interest to examine the response ofM. tuberculosis to DNA damage. The expression ofrecA, a key component in DNA repair and recombination, is induced by DNA damage in M. tuberculosis. In this study, we have analyzed the expression following DNA damage in M. tuberculosis of a number of other genes which are DNA damage inducible in Escherichia coli. While many of these genes were also induced by DNA damage in M. tuberculosis, some were not. In a
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Kunisch, Ralph, Elisabeth Kamal, and Astrid Lewin. "The role of the mycobacterial DNA-binding protein 1 (MDP1) from Mycobacterium bovis BCG in host cell interaction." BMC Microbiology 12, no. 1 (2012): 165. http://dx.doi.org/10.1186/1471-2180-12-165.

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27

Chaitra, M. G., M. S. Shaila, and R. Nayak. "Evaluation of T-cell responses to peptides with MHC class I-binding motifs derived from PE_PGRS 33 protein of Mycobacterium tuberculosis." Journal of Medical Microbiology 56, no. 4 (2007): 466–74. http://dx.doi.org/10.1099/jmm.0.46928-0.

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The PE and PPE proteins of Mycobacterium tuberculosis form a source of antigenic variation among different strains of M. tuberculosis. One of the PE_PGRS proteins, Rv1818c, plays a role in the pathogenesis of mycobacterial infection and specifically influences host-cell responses to tuberculosis infection. Although little is known about these two classes of protein, an immunoinformatics approach has indicated the possibility of their participation in eliciting a major histocompatibility complex (MHC) class I-mediated immune response against tuberculosis, as peptides derived from Rv1818c are pr
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28

Wei, Jun, John L. Dahl, James W. Moulder, et al. "Identification of a Mycobacterium tuberculosis Gene That Enhances Mycobacterial Survival in Macrophages." Journal of Bacteriology 182, no. 2 (2000): 377–84. http://dx.doi.org/10.1128/jb.182.2.377-384.2000.

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ABSTRACT Intracellular survival plays a central role in the pathogenesis ofMycobacterium tuberculosis. To identify M. tuberculosis genes required for intracellular survival within macrophages, an M. tuberculosis H37Rv plasmid library was constructed by using the shuttle vector pOLYG. This plasmid library was electroporated into Mycobacterium smegmatis 1-2c, and the transformants were used to infect the human macrophage-like cell line U-937. Because M. smegmatis does not readily survive within macrophages, any increased intracellular survival is likely due to cloned M. tuberculosis H37Rv DNA. A
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29

Janowski, Robert, Santosh Panjikar, Ali Nasser Eddine, Stefan H. E. Kaufmann, and Manfred S. Weiss. "Structural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosis." Journal of Structural and Functional Genomics 10, no. 2 (2009): 137–50. http://dx.doi.org/10.1007/s10969-009-9060-4.

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Datta, S., R. Krishna, N. Ganesh, Nagasuma R. Chandra, K. Muniyappa, and M. Vijayan. "Crystal Structures of Mycobacterium smegmatis RecA and Its Nucleotide Complexes." Journal of Bacteriology 185, no. 14 (2003): 4280–84. http://dx.doi.org/10.1128/jb.185.14.4280-4284.2003.

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ABSTRACT The crystal structures of Mycobacterium smegmatis RecA (RecAMs) and its complexes with ADP, ATPγS, and dATP show that RecAMs has an expanded binding site like that in Mycobacterium tuberculosis RecA, although there are small differences between the proteins in their modes of nucleotide binding. Nucleotide binding is invariably accompanied by the movement of Gln 196, which appears to provide the trigger for transmitting the effect of nucleotide binding to the DNA-binding loops. These observations provide a framework for exploring the known properties of the RecA proteins.
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Rodrigue, Sébastien, Joëlle Brodeur, Pierre-Étienne Jacques, Alain L. Gervais, Ryszard Brzezinski та Luc Gaudreau. "Identification of Mycobacterial σ Factor Binding Sites by Chromatin Immunoprecipitation Assays". Journal of Bacteriology 189, № 5 (2006): 1505–13. http://dx.doi.org/10.1128/jb.01371-06.

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ABSTRACT Mycobacterium tuberculosis and Mycobacterium bovis are responsible for infections that cause a substantial amount of death, suffering, and loss around the world. Still, relatively little is known about the mechanisms of gene expression in these bacteria. Here, we used genome-wide location assays to identify direct target genes for mycobacterial σ factors. Chromatin immunoprecipitation assays were performed with M. bovis BCG for Myc-tagged proteins expressed using an anhydrotetracycline-inducible promoter, and enriched DNA fragments were hybridized to a microarray representing intergen
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Rex, Kervin, Sanjay Kumar Bharti, Shivjee Sah, and Umesh Varshney. "A Genetic Analysis of the Functional Interactions within Mycobacterium tuberculosis Single-Stranded DNA Binding Protein." PLoS ONE 9, no. 4 (2014): e94669. http://dx.doi.org/10.1371/journal.pone.0094669.

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33

Prasad, H. K., S. Prabhakar, P. S. Annapurna, et al. "DNA binding protein of mycobacteria and human immune response." Indian Journal of Clinical Biochemistry 12, S1 (1997): 86–88. http://dx.doi.org/10.1007/bf02873070.

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34

Blokpoel, Marian C. J., Marjan J. Smeulders, Julia A. M. Hubbard, Jacquie Keer, and Huw D. Williams. "Global Analysis of Proteins Synthesized by Mycobacterium smegmatis Provides Direct Evidence for Physiological Heterogeneity in Stationary-Phase Cultures." Journal of Bacteriology 187, no. 19 (2005): 6691–700. http://dx.doi.org/10.1128/jb.187.19.6691-6700.2005.

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ABSTRACT We have characterized the induction kinetics of ∼1,700 proteins during entry into and survival in carbon-starved stationary phase by Mycobacterium smegmatis. Strikingly, among the patterns of expression observed were a group of proteins that were expressed in exponential-phase cultures and severely repressed in 48-h stationary-phase cultures (Spr or stationary-phase-repressed proteins) but were synthesized again at high levels in ≥128-day stationary-phase cultures (Spr128↑ proteins). A number of Spr128↑ proteins were identified, and they included the heat shock protein DnaK, the trica
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Acharya, Narottam, and Umesh Varshney. "Biochemical Properties of Single-Stranded DNA-Binding Protein from Mycobacterium smegmatis, a Fast-growing Mycobacterium and Its Physical and Functional Interaction with Uracil DNA Glycosylases." Journal of Molecular Biology 318, no. 5 (2002): 1251–64. http://dx.doi.org/10.1016/s0022-2836(02)00053-0.

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Dias, Andre, Camila Silva, Carlos Adriano Silva, João Pedro Santos, Geraldo Pereira, and Maria Cristina Pessolani. "The involvement of Mycobacterium leprae Hlp-DNA complex in bacterial recognition and airways epithelial activation (INM3P.404)." Journal of Immunology 194, no. 1_Supplement (2015): 127.9. http://dx.doi.org/10.4049/jimmunol.194.supp.127.9.

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Abstract Airways are considered the main site of entry of Mycobacterium leprae (ML), the causative agent of leprosy. ML expresses a histone-like protein (Hlp), present in the cell envelope, which has been implicated in the binding of this mycobacterium to respiratory epithelial cells (ECs). So we investigated whether mycobacterial DNA-Hlp complexes are able to increase the human alveolar epithelial cell line A549 responses to ML through recognition by TLR9. ELISA results showed that ML and soluble CpG-Hlp complexes increase IL-8 secretion in ECs. Moreover, immunoblotting and ELISA assays revea
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Fivian-Hughes, Amanda S., and Elaine O. Davis. "Analyzing the Regulatory Role of the HigA Antitoxin within Mycobacterium tuberculosis." Journal of Bacteriology 192, no. 17 (2010): 4348–56. http://dx.doi.org/10.1128/jb.00454-10.

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ABSTRACT Bacterial chromosomally encoded type II toxin-antitoxin (TA) loci may be involved in survival upon exposure to stress and have been linked to persistence and dormancy. Therefore, understanding the role of the numerous predicted TA loci within the human pathogen Mycobacterium tuberculosis has become a topic of great interest. Antitoxin proteins are known to autoregulate TA expression under normal growth conditions, but it is unknown whether they have a more global role in transcriptional regulation. This study focuses on analyzing the regulatory role of the M. tuberculosis HigA antitox
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38

Watkins, Harriet A., and Edward N. Baker. "Structural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosis." Journal of Bacteriology 192, no. 11 (2010): 2878–86. http://dx.doi.org/10.1128/jb.01615-09.

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ABSTRACT The open reading frame Rv2228c from Mycobacterium tuberculosis is predicted to encode a protein composed of two domains, each with individual functions, annotated through sequence similarity searches. The N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with α-ribazole phosphatase (CobC). The N-terminal domain of Rv2228c (Rv2228c/N) and the full-length protein were expressed as fusions with maltose binding protein (MBP). Rv2228c/N was shown to have RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase
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39

Kwofie, Samuel K., Kweku S. Enninful, Jaleel A. Yussif, et al. "Molecular Informatics Studies of the Iron-Dependent Regulator (ideR) Reveal Potential Novel Anti-Mycobacterium ulcerans Natural Product-Derived Compounds." Molecules 24, no. 12 (2019): 2299. http://dx.doi.org/10.3390/molecules24122299.

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Buruli ulcer is a neglected tropical disease caused by the bacterium Mycobacterium ulcerans. Its virulence is attributed to the dermo-necrotic polyketide toxin mycolactone, whose synthesis is regressed when its iron acquisition system regulated by the iron-dependent regulator (ideR) is deactivated. Interfering with the activation mechanism of ideR to inhibit the toxin’s synthesis could serve as a possible cure for Buruli ulcer. The three-dimensional structure of the ideR for Mycobacterium ulcerans was generated using homology modeling. A library of 832 African natural products (AfroDB), as wel
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40

David, M., S. Lubinsky-Mink, A. Ben-Zvi, M. Suissa, S. Ulitzur, and J. Kuhn. "Citrate synthase from Mycobacterium smegmatis. Cloning, sequence determination and expression in Escherichia coli." Biochemical Journal 278, no. 1 (1991): 225–34. http://dx.doi.org/10.1042/bj2780225.

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A Mycobacterium smegmatis PstI library was constructed by cloning these fragments downstream from the lac promoter of the expression vector pHG171. Three identically sized clones were isolated by complementation of an Escherichia coli strain (chi 2338) deficient in citrate synthase. One insert (pBL265) was used in hybridization experiments with DNA from E. coli and M. smegmatis and it was demonstrated that the clones were indeed from M. smegmatis. The transcription of the M. smegmatis citrate synthase gene in E. coli relied upon the lac promoter. In translation experiments performed in vitro p
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41

Saikrishnan, K., J. Jeyakanthan, J. Venkatesh, et al. "Structure of Mycobacterium tuberculosis Single-stranded DNA-binding Protein. Variability in Quaternary Structure and Its Implications." Journal of Molecular Biology 331, no. 2 (2003): 385–93. http://dx.doi.org/10.1016/s0022-2836(03)00729-0.

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42

Purnapatre, Kedar, and Umesh Varshney. "Cloning, over-expression and biochemical characterization of the single-stranded DNA binding protein from Mycobacterium tuberculosis." European Journal of Biochemistry 264, no. 2 (1999): 591–98. http://dx.doi.org/10.1046/j.1432-1327.1999.00684.x.

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43

Anand, Chinmay, Rajni Garg, Soumitra Ghosh, and Valakunja Nagaraja. "A Sir2 family protein Rv1151c deacetylates HU to alter its DNA binding mode in Mycobacterium tuberculosis." Biochemical and Biophysical Research Communications 493, no. 3 (2017): 1204–9. http://dx.doi.org/10.1016/j.bbrc.2017.09.087.

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44

Richardson, William, Gyun Won Kang, Hee Joong Lee, Kang Mu Kwon, Saron Kim, and Hyo Jung Kim. "Chasing the structural diversity of the transcription regulator Mycobacterium tuberculosis HigA2." IUCrJ 8, no. 5 (2021): 823–32. http://dx.doi.org/10.1107/s2052252521007715.

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Transcription factors are the primary regulators of gene expression and recognize specific DNA sequences under diverse physiological conditions. Although they are vital for many important cellular processes, it remains unclear when and how transcription factors and DNA interact. The antitoxin from a toxin–antitoxin system is an example of negative transcriptional autoregulation: during expression of the cognate toxin it is suppressed through binding to a specific DNA sequence. In the present study, the antitoxin HigA2 from Mycobacterium tuberculosis M37Rv was structurally examined. The crystal
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Zhang, Hua, Yuxi Tian, Ziduo Liu, Feng Huang, Lihua Hu, and Zheng-Guo He. "Characterization of amino acid residues essential for tetramer formation and DNA-binding activity of ssDNA-binding protein of Mycobacterium tuberculosis." Biochemistry (Moscow) 76, no. 6 (2011): 658–65. http://dx.doi.org/10.1134/s000629791106006x.

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46

Ruswanto, Ruswanto, Nur Rahayuningsih, Nur Laeli Dwi Hidayati, Ginna Sri Nuryani, and Richa Mardianingrum. "Uji In Vitro dan Studi In Silico Senyawa Turunan n’-benzoylisonicotinohydr." JURNAL ILMU KEFARMASIAN INDONESIA 17, no. 2 (2019): 218. http://dx.doi.org/10.35814/jifi.v17i2.703.

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Telah dilakukannya penelitian tentang studi in vitro dan in silico senyawa turunan N-Benzoylisonicotinohydrazide. Penelitian ini bertujuan untuk mengetahui bahwa senyawa turunan N’-benzoylisonicotinohydrazide dapat menghambat aktivitas bakteri gram positif, gram negatif dan Mycobacterium tuberculosis, serta mempunyai interaksi yang baik dengan Enoyl-Acyl Carrier Protein Reductase dari Mycobacterium Tuberculosis. Dari uji in vitro dihasilkan bahwa senyawa N’-benzoylisonicotinohydrazide memiliki Minimum Inhibitor Concentration (MIC) sebesar 0,33 µg/ml terhadap bakteri Basillus subtilis, sedangka
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47

Chandran, A. V., R. Srikalaivani, A. Paul, and M. Vijayan. "Biochemical characterization of Mycobacterium tuberculosis LexA and structural studies of its C-terminal segment." Acta Crystallographica Section D Structural Biology 75, no. 1 (2019): 41–55. http://dx.doi.org/10.1107/s2059798318016066.

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LexA is a protein that is involved in the SOS response. The protein from Mycobacterium tuberculosis and its mutants have been biochemically characterized and the structures of their catalytic segments have been determined. The protein is made up of an N-terminal segment, which includes the DNA-binding domain, and a C-terminal segment encompassing much of the catalytic domain. The two segments are defined by a cleavage site. Full-length LexA, the two segments, two point mutants involving changes in the active-site residues (S160A and K197A) and another mutant involving a change at the cleavage
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48

Haydel, Shelley E., William H. Benjamin, Nancy E. Dunlap, and Josephine E. Clark-Curtiss. "Expression, Autoregulation, and DNA Binding Properties of the Mycobacterium tuberculosis TrcR Response Regulator." Journal of Bacteriology 184, no. 8 (2002): 2192–203. http://dx.doi.org/10.1128/jb.184.8.2192-2203.2002.

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ABSTRACT The TrcRS two-component system of Mycobacterium tuberculosis is comprised of the TrcS histidine kinase and the TrcR response regulator, which is homologous to the OmpR class of DNA binding response regulators. Reverse transcription-PCRs with total RNA showed that the trcR and trcS two-component system genes are transcribed in broth-grown M. tuberculosis. Analysis of the trcR and trcS genes using various SCOTS (selective capture of transcribed sequences) probes also confirmed that these genes are expressed in broth-grown cultures and after 18 h of M. tuberculosis growth in cultured hum
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49

Amon, Johannes, Tanja Bräu, Aletta Grimrath, et al. "Nitrogen Control in Mycobacterium smegmatis: Nitrogen-Dependent Expression of Ammonium Transport and Assimilation Proteins Depends on the OmpR-Type Regulator GlnR." Journal of Bacteriology 190, no. 21 (2008): 7108–16. http://dx.doi.org/10.1128/jb.00855-08.

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ABSTRACT The effect of nitrogen regulation on the level of transcriptional control has been investigated in a variety of bacteria, such as Bacillus subtilis, Corynebacterium glutamicum, Escherichia coli, and Streptomyces coelicolor; however, until now there have been no data for mycobacteria. In this study, we found that the OmpR-type regulator protein GlnR controls nitrogen-dependent transcription regulation in Mycobacterium smegmatis. Based on RNA hybridization experiments with a wild-type strain and a corresponding mutant strain, real-time reverse transcription-PCR analyses, and DNA binding
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50

Yeruva, Veena C., Sridevi Duggirala, V. Lakshmi, Daniel Kolarich, Friedrich Altmann, and Manjula Sritharan. "Identification and Characterization of a Major Cell Wall-Associated Iron-Regulated Envelope Protein (Irep-28) in Mycobacterium tuberculosis." Clinical and Vaccine Immunology 13, no. 10 (2006): 1137–42. http://dx.doi.org/10.1128/cvi.00125-06.

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ABSTRACTIron limitation and the expression of mycobactin and carboxymycobactin byMycobacterium tuberculosisare known. Here, we report how iron regulated the coordinate expression of these two siderophores and a 28-kDa cell wall-associated iron-regulated protein (Irep-28). Irep-28 is identified as the DNA-binding HU homologue HupB protein (hupB[Rv2986c]). Antibodies to this protein were detected in sera from tuberculosis patients. The location of the protein in the cell wall makes it a potential drug target.
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