Publications

Ojo, O., Scott, D., Furlong, B., Iwalokun, B., Odetoyin, B. and Grove, A. Transcriptome RNA Sequencing Data Set of Differential Gene Expression in Escherichia coli BW25113 Wild Type and slyA Mutant Strains. (2021). Microbiol. Resour. Announc. 10, e00294-21.

Sivapragasam, S., Ghosh, A., Kumar, S., Johnson, D. T., Grove, A. Similar solutions to a common challenge: Regulation of genes encoding Ralstonia solanacearum xanthine dehydrogenase (2021). FEMS Microbiol. Lett. 368, fnab022.

Kumar, S., Mashkoor, M., Balamurugan, P. and Grove, A. Intricate regulation of ribosome biogenesis genes in response to mTORC1 signaling. (2021). bioRxiv.

Thapa, S. S. and Grove, A. Impaired purine homeostasis plays a primary role in trimethoprim-mediated induction of virulence genes in Burkholderia thailandensis. (2021). Mol. Microbiol. 115, 610-622

Thapa, S. S. and Grove, A. Do global regulators hold the key to production of bacterial secondary metabolites? (2019). Antibiotics 8, 160.

Sivapragasam, S. and Grove, A. The link between purine metabolism and production of antibiotics in Streptomyces. (2019). Antibiotics 8, 76.

Deochand, D. K., Pande, A., Meariman, J. K. and Grove, A. Redox-sensing by PecS from the plant pathogen Pectobacterium atrosepticum and its effect on gene expression and the conformation of PecS-bound promoter DNA. (2019). Biochemistry58, 2564-2575.

Bhattacharyya, N., Lemon, T. L. and Grove, A. A role for Vibrio vulnificus PecS during hypoxia. (2019). Sci. Rep. 9, 2797.

Sabrin, A., Gioe, B. W., Gupta, A. and Grove, A. An EmrB multidrug efflux pump in Burkholderia thailandensis with unexpected roles in antibiotic resistance. (2019). J. Biol. Chem. 294, 1891-1903. Selected for inclusion in Virtual Issue on Antibiotic resistance

Gupta, A., Pande, A., Sabrin, A., Thapa, S. S., Gioe, B. W. and Grove, A. MarR family transcription factors from Burkholderia species: Hidden clues to control of virulence-associated genes. (2019). Microbiol. Mol. Biol. Rev. 83, e00039-18.

Pande, A., Veale, T. C. and Grove, A. Gene regulation by redox-sensitive Burkholderia thailandensis OhrR and its role in bacterial killing of Caenorhabditis elegans. (2018). Infect. Immun. 86, e00322-18.

Grove, A. Control of RNA polymerase II-transcribed genes by direct binding of TOR kinase. (2018). Curr. Genet. 64, 131-135.

Gupta, A., Bedre, R, Thapa, S. S., Sabrin, A., Wang, G., Dassanayake, M. and Grove, A. Global awakening of cryptic biosynthetic gene clusters in Burkholderia thailandensis. (2017). ACS Chem. Biol. 12, 3012-3021.

Sivapragasam, S., Deochand, D. K., Meariman, J. K. and Grove, A. Stringent response induced by phosphate limitation promotes purine salvage in Agrobacterium fabrum. (2017). Biochemistry 56, 5831-5843.

Vidanapathirana, P., Hasan, F., Mussio, K., Pande, A., Brands, M., Siraj, N., Grove, A. and Warner, I. M. Cationic Ionic Liquid Surfactant-Polyacrylamide Gel Electrophoresis for Enhanced Separation of Acidic and Basic Proteins with Single-Step Ribonuclease b Glycoforms Separation. (2017). J. Chromatogr. A 1515, 245-251.

Panday, A., Gupta, A., Srinivasa, K., Xiao, L., Smith, M. D. and Grove, A. DNA damage regulates direct association of TOR kinase with the RNA polymerase II-transcribed HMO1 gene. (2017). Mol. Biol. Cell. 28, 2449-2459.

Deochand, D. K. and Grove, A. MarR family transcription factors: Dynamic variations on a common scaffold. (2017). Crit. Rev. Biochem. Mol. Biol. 52, 595-613.

Grove, A. Regulation of metabolic pathways by MarR family transcription factors. (2017). Comp. Struct. Biotechnol. J. 15, 366-371.

Gupta, A., Fuentes, S. and Grove, A. Redox-sensitive MarR homologue BifR from Burkholderia thailandensis regulates biofilm formation. (2017). Biochemistry 56, 2315-2327.

Panday, A., Xiao, L., Gupta, A. and Grove, A. Control of DNA end resection by yeast Hmo1p affects efficiency of DNA end-joining. (2017). DNA Repair 53, 15-23.

Panday, A. and Grove, A. Yeast HMO1 – linker histone reinvented. (2017). Microbiol. Mol. Biol. Rev. 81:e00037-16.

Sivapragasam, S. and Grove, A. Determination of (p)ppGpp Levels During Stringent Response in Streptomyces coelicolor by Thin Layer Chromatography. (2016). Bio-protocol. 6(21):e1995.

Deochand, D. K., Perera, I. C., Crochet, R. B., Gilbert, N. C., Newcomer, M. E. and Grove, A. Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices. (2016). Mol. BioSyst. 12, 2417-2426.

Deochand, D. K., Meariman, J. K. and Grove, A. pH-dependent regulation of gene expression by Pectobacterium atrosepticum PecS. (2016). ACS Chem. Biol. 11, 2049-2056.

Panday, A. and Grove, A. The high mobility group protein HMO1 functions as a linker histone in yeast. (2016). Epigenetics Chromatin 9:13.

Sivapragasam, S. and Grove, A. Streptomyces coelicolor XdhR is a direct target of (p)ppGpp that controls expression of genes encoding xanthine dehydrogenase to promote purine salvage. (2016). Mol. Microbiol. 100, 701-718.

Panday, A., Xiao, L. and Grove, A. Yeast high mobility group protein HMO1 stabilizes chromatin and is evicted during repair of DNA double strand breaks. (2015). Nucleic Acids Res. 43, 5759-5770.

Sivapragasam, S., Pande, A. and Grove, A. A recommended workflow for DNase I footprinting using a capillary electrophoresis genetic analyzer. (2015). Anal. Biochem. 481, 1-3.

Huang, H., Sivapragasam, S. and Grove, A. The regulatory role of Streptomyces coelicolor TamR in central metabolism. (2015). Biochem. J. 466, 347-358.

Kushwaha, A. K., Deochand, D. K. and Grove, A. A moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis? (2015). Protein Sci. 24, 253-263.

Grove, A., Kushwaha, A. K. and Nguyen, K. H. Determining the role of metal binding in protein cage assembly. (2015). Methods Mol. Biol. 1252, 91-100.

Gupta, A. and Grove, A. Ligand binding pocket bridges DNA-binding and dimerization domains of the urate-responsive MarR homologue MftR from Burkholderia thailandensis. (2014). Biochemistry 53, 4368-4380.

Xiao, L. and Grove, A. Role of HMGB proteins in coordinating ribosomal protein and ribosomal RNA gene expression in response to TOR signaling. (2013). In: Advances in Genome Science: Probing intracellular regulation (C. Néri, ed.). Vol. 2, pp. 155-175. Bentham Science.

Kushwaha, A. K. and Grove, A. Mycobacterium smegmatis Ku binds DNA without free ends. (2013). Biochem. J. 456, 275-282.

Huang, H., Mackel, B. J. and Grove, A. Streptomyces coelicolor encodes a urate-responsive transcriptional regulator with homology to PecS from plant pathogens. (2013). J. Bacteriol. 195, 4954-4965.

Grove, A. MarR family transcription factors. (2013). Curr. Biol. 23, R142-143.

Huang, H. and Grove, A. The transcriptional regulator TamR from Streptomyces coelicolor controls a key step in central metabolism during oxidative stress. (2013). Mol. Microbiol. 87, 1151-1166.

Kushwaha, A. K. and Grove, A. C-terminal low-complexity sequence repeats of Mycobacterium smegmatis Ku modulate DNA binding. (2013).Biosci. Rep. 33, e00016.

Reon, B. J., Nguyen, K. H., Bhattacharyya, G and Grove, A. Functional comparison of Deinococcus radiodurans Dps proteins suggests distinct in vivo roles. (2012). Biochem. J. 447, 381-391.

Nguyen, K. H. and Grove, A. Metal binding at the Deinococcus radiodurans Dps-1 N-terminal metal site controls dodecameric assembly and DNA binding. (2012). Biochemistry 51, 6679-6689.

Ray, S. and Grove, A. Interaction of Saccharomyces cerevisiae HMO2 domains with distorted DNA. (2012). Biochemistry 51, 1825-1835.

Nguyen, K. H., Smith, L. T., Xiao, L., Bhattacharyya, G. and Grove, A. On the stoichiometry of Deinococcus radiodurans Dps-1 binding to duplex DNA. (2012). Proteins 80, 713-721.

Xiao, L., Kamau, E., Donze, D. and Grove, A. Expression of yeast high mobility group protein HMO1 is regulated by TOR signaling. (2011).Gene 489, 55-62.

Perera, I. C. and Grove, A. MarR homologs with urate-binding signature. (2011). Protein Sci. 20, 621-629.

Grove, A. Functional evolution of bacterial histone-like HU proteins. (2011). Curr. Issues Mol. Biol. 13, 1-11.

Grove, A. Urate-responsive MarR homologs from Burkholderia. (2010). Mol. Biosyst. 6, 2133-2142.

Perera, I. C. and Grove, A. Urate is a ligand for the transcriptional regulator PecS. (2010). J. Mol. Biol. 402, 571-583.

Perera, I. C. and Grove, A. Molecular mechanisms of ligand-mediated attentuation of DNA binding by MarR family transcriptional regulators. (2010). J. Mol. Cell Biol. 2, 243-254. Cover Article.

Xiao, L., Williams, A. M. and Grove, A. The C-terminal domain of yeast high mobility group protein HMO1 mediates lateral protein accretion and in-phase DNA bending. (2010). Biochemistry 49, 4051–4059.

Wowor, A. J., Datta, K., Brown, H. S., Thompson, G. S., Ray, S., Grove, A. and LiCata, V. J. Thermodynamics of the DNA structural selectivity of the Pol I DNA polymerases from Escherichia coli and Thermus aquaticus. (2010). Biophys. J. 98, 3015-3024.

Meades, Jr., G., Benson, B. K., Grove, A. and Waldrop, G. L. A tale of two functions: Enzymatic activity and translational repression by carboxyltransferase. (2010). Nucleic Acids Res. 38, 1217-1227.

Ray, S. and Grove, A. The yeast high mobility group protein HMO2, a subunit of the chromatin remodeling complex INO80, binds DNA ends. (2009). Nucleic Acids Res. 37, 6389–6399.

Perera, I. C., Lee, Y.-H., Wilkinson, S. P. and Grove, A. Mechanism for attenuation of DNA binding by MarR family transcriptional regulators by small molecule ligands. (2009). J. Mol. Biol. 390, 1019–1029.

Xiao, L. and Grove, A. Coordination of ribosomal protein and ribosomal RNA gene expression in response to TOR signaling. (2009). Curr. Genomics 10, 198-205.

Jain, T., Roper, B. J. and Grove, A. A Functional Type I Topoisomerase from Pseudomonas aeruginosa. (2009). BMC Mol. Biol. 10, 23.

Mukherjee, A., DiMario, P. J. and Grove, A. Mycobacterium smegmatis histone-like protein Hlp is nucleoid associated. (2009). FEMS Microbiol. Lett. 291, 232-240.

Mukherjee, A. Bhattacharyya, G. and Grove, A. The C-terminal domain of Mycobacterium smegmatis histone-like protein mediates DNA end-joining and is required for transcriptional repression. (2008). Biochemistry 47, 8744-8753.

Mukherjee, A., Sokunbi, A. O. and A. Grove, A. DNA protection by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima. (2008). Nucleic Acids Res. 36, 3956-3968.

Benson, B. K., Meades, G., Grove, A. and Waldrop G. L. DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: Implications for active site communication. (2008). Protein Sci. 17, 34-42.

Bhattacharyya,G. and Grove, A. The N-terminal extensions of Deinococcus radiodurans Dps-1 mediate DNA major groove interactions as well as assembly of the dodecamer. (2007). J. Biol. Chem. 282, 11921-11930.

Tsihlis, N. D. and Grove, A. The Saccharomyces cerevisiae RNA polymerase III recruitment factor subunits Brf1 and Bdp1 impose a strict sequence preference for the downstream half of the TATA box. (2006). Nucleic Acids Res. 34, 5585-5593.

Kim, S.-G., Bhattacharyya, G., Grove, A. and Lee, Y.-H. Crystal Structure of Dps-1, a Functionally Distinct Dps Protein from Deinococcus radiodurans. (2006). J. Mol. Biol. 361, 105-114.

Bordelon, T., Wilkinson, S. P., Grove, A. and Newcomer, M. E. The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding. (2006). J. Mol. Biol. 360, 168-177.

Bauerle, K. T., Kamau, E. and Grove, A. Interactions between the N- and C-terminal domains of the Saccharomyces cerevisiae high mobility group protein HMO1 are required for DNA bending. (2006). Biochemistry 45, 3635-3645.

Ghosh, S. and Grove, A. The Deinococcus radiodurans-encoded HU protein has two DNA-binding domains. (2006). Biochemistry 45,1723-1733.

Wilkinson, S. P. and Grove, A. Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins. (2006). Curr. Issues Mol. Biol. 8, 51-62.

Wilkinson, S. P. and Grove, A. Negative cooperativity of uric acid binding to the transcriptional regulator HucR from Deinococcus radiodurans. (2005). J. Mol. Biol. 350, 617-630.

Kamau, E., Tsihlis, N. D., Simmons, L. A., and Grove, A. Surface salt bridges modulate DNA site size of bacterial histone-like HU proteins. (2005). Biochem. J. 390, 49-55.

Grove, A. and Wilkinson, S. P. Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans. (2005). J. Mol. Biol. 347, 495-508.

Kamau, E., Bauerle, K. T. and Grove, A. The Saccharomyces cerevisiae HMGB protein HMO1 contains two functional DNA-binding domains. (2004). J. Biol. Chem. 279, 55234-55240.

Wilkinson, S. P. and Grove, A. HucR, a novel uric acid responsive member of the MarR family of transcriptional regulators from Deinococcus radiodurans. (2004). J. Biol. Chem. 279, 51442-51450.

Kamau, E. and Grove, A. Fluoroquinolone-dependent DNA supercoiling by Vaccinia topoisomerase I. (2004). J. Mol. Biol. 342, 479-487.

Chen, C., Ghosh, S. and Grove, A. Substrate specificity of Helicobacter pylori HU is determined by insufficient stabilization of DNA flexure points. (2004). Biochem. J. 383, 343-35.

Ghosh, S. and Grove, A. Histone-like protein HU from Deinococcus radiodurans binds preferentially to four-way DNA junctions. (2004). J. Mol. Biol. 337, 561-571.

Grove, A. Gene regulation: Eukaryotes. (2004). In: Encyclopedia of Genetics (Ness, B., Ed.), pp. 295-298. Salem Press, CA.

Grove, A. Surface salt bridges modulate DNA wrapping by the Type II DNA binding protein TF1. (2003). Biochemistry 42, 8739-8747.

Kassavetis, G. A., Grove, A. and Geiduschek, E. P. Effects of DNA strand breaks on transcription by RNA polymerase III: insights into the role of TFIIIB and the polarity of promoter opening. (2002). EMBO J. 21, 5506-5515.

Grove, A. and Saavedra, T. C. The role of surface-exposed lysines in wrapping DNA about the bacterial histone-like protein HU. (2002). Biochemistry 41, 7597-7603.

Grove, A., Adessa, M. S., Geiduschek, E. P. and Kassavetis, G. A. Marking the start site of RNA polymerase III transcription: the role of constraint, compaction and continuity of the transcribed DNA strand. (2002). EMBO J. 21, 704-714.

Grove, A. and Lim, L. High-affinity DNA binding of HU protein from the hyperthermophile Thermotoga maritima. (2001). J. Mol. Biol. 311, 491-502.

Vu, H. M., Liu, W., Grove, A., Geiduschek, E. P. and Kearns, D. R. Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 as explained by 1H, 15N and 13C NMR chemical shifts and secondary structure analysis. (2000). Biochem. Biophys. Acta 1478, 113-124.

Grove, A., Kassavetis, G. A., Johnson, T. E. and Geiduschek, E. P. The RNA polymerase III-recruiting factor TFIIIB induces a DNA bend between the TATA box and the transcriptional start site. (1999). J. Mol. Biol. 285, 1429-1440.

Grove, A., Galeone, A., Yu, E., Mayol, L. and Geiduschek, E. P. Affinity, stability and polarity of binding of the TATA binding protein governed by flexure at the TATA box. (1998). J. Mol. Biol. 282, 731-739.

Kumar, A., Grove, A., Kassavetis, G. A. and Geiduschek, E. P. Transcription Factor IIIB: The architecture of its DNA complex, and its roles in initiation of transcription by RNA polymerase III. In: Cold Spring Harbor Symposia on Quantitative Biology: Mechanisms of Transcription. Vol. LXIII, pp. 121-129. Cold Spring Harbor Laboratory Press (1998).

Grove, A., Figueiredo, M. L., Galeone, A., Mayol, L. and Geiduschek, E. P. Twin hydroxymethyluracil-A basepair steps define the binding site for the DNA-bending protein TF1. (1997). J. Biol. Chem. 272, 13084-13087.

Grove, A. and Geiduschek, E. P. Localizing flexibility within the target site of DNA-bending proteins. (1997). In: Techniques in Protein Chemistry vol. VIII (D. M. Marshak, ed.), pp. 585-592. Academic Press.

Jia, X., Grove, A., Ivancic, M., Hsu, V. L., Geiduschek, E. P. and Kearns, D. R. Structure of the Bacillus subtilis phage SPO1-encoded type II DNA-binding protein TF1 in solution. (1996). J. Mol. Biol. 263, 259-268.

Grove, A., Galeone, A., Mayol, L. and Geiduschek, E. P. On the connection between inherent DNA flexure and preferred binding of hydroxymethyluracil-containing DNA by the type II DNA-binding protein TF1. (1996). J. Mol. Biol. 206, 196-206.

Grove, A., Galeone, A., Mayol, L. and Geiduschek, E. P. Localized DNA flexibility contributes to target site selection by DNA-bending proteins. (1996). J. Mol. Biol. 206, 120-125.