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Volumn 196, Issue 2, 2014, Pages 265-275

The YmdB phosphodiesterase is a global regulator of late adaptive responses in bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; PHOSPHODIESTERASE;

EID: 84890926407     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00826-13     Document Type: Article
Times cited : (53)

References (64)
  • 1
    • 0035340694 scopus 로고    scopus 로고
    • The biofilm matrix-an immobilized but dynamic microbial environment
    • Sutherland IW. 2001. The biofilm matrix-an immobilized but dynamic microbial environment. Trends Microbiol. 9:222-227. http://dx.doi.org/10.1016/S0966-842X(01)02012-1.
    • (2001) Trends Microbiol. , vol.9 , pp. 222-227
    • Sutherland, I.W.1
  • 2
    • 0037154837 scopus 로고    scopus 로고
    • Extracellular DNA required for bacterial biofilm formation
    • Whitchurch CB, Tolker-Nielsen T, Ragas PC, Mattick JS. 2002. Extracellular DNA required for bacterial biofilm formation. Science 295:1487. http://dx.doi.org/10.1126/science.295.5559.1487.
    • (2002) Science , vol.295 , pp. 1487
    • Whitchurch, C.B.1    Tolker-Nielsen, T.2    Ragas, P.C.3    Mattick, J.S.4
  • 4
    • 84864091339 scopus 로고    scopus 로고
    • A Bacillus subtilis sensor kinase involved in triggering biofilm formation on the roots of tomato plants
    • Chen Y, Cao S, Chai Y, Clardy J, Kolter R, Guo JH, Losick R. 2012. A Bacillus subtilis sensor kinase involved in triggering biofilm formation on the roots of tomato plants. Mol. Microbiol. 85:418-430. http://dx.doi.org/10.1111/j.1365-2958.2012.08109.x.
    • (2012) Mol. Microbiol. , vol.85 , pp. 418-430
    • Chen, Y.1    Cao, S.2    Chai, Y.3    Clardy, J.4    Kolter, R.5    Guo, J.H.6    Losick, R.7
  • 5
    • 79955427250 scopus 로고    scopus 로고
    • Tracing the domestication of a biofilm-forming bacterium
    • McLoon AL, Guttenplan SB, Kearns DB, Kolter R, Losick R. 2011. Tracing the domestication of a biofilm-forming bacterium. J. Bacteriol. 193:2027-2034. http://dx.doi.org/10.1128/JB.01542-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 2027-2034
    • McLoon, A.L.1    Guttenplan, S.B.2    Kearns, D.B.3    Kolter, R.4    Losick, R.5
  • 6
    • 33646011232 scopus 로고    scopus 로고
    • Effects of phosphorelay perturbations on architecture, sporulation, and spore resistance in biofilms of Bacillus subtilis
    • Veening JW, Kuipers OP, Brul S, Hellingwerf KJ, Kort R. 2006. Effects of phosphorelay perturbations on architecture, sporulation, and spore resistance in biofilms of Bacillus subtilis. J. Bacteriol. 188:3099-3109. http://dx.doi.org/10.1128/JB.188.8.3099-3109.2006.
    • (2006) J. Bacteriol. , vol.188 , pp. 3099-3109
    • Veening, J.W.1    Kuipers, O.P.2    Brul, S.3    Hellingwerf, K.J.4    Kort, R.5
  • 7
    • 79551482850 scopus 로고    scopus 로고
    • Rok regulates yuaB expression during architecturally complex colony development of Bacillus subtilis 168
    • Kovacs AT, Kuipers OP. 2011. Rok regulates yuaB expression during architecturally complex colony development of Bacillus subtilis 168. J. Bacteriol. 193:998-1002. http://dx.doi.org/10.1128/JB.01170-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 998-1002
    • Kovacs, A.T.1    Kuipers, O.P.2
  • 8
    • 13444292348 scopus 로고    scopus 로고
    • A master regulator for biofilm formation by Bacillus subtilis
    • Kearns DB, Chu F, Branda SS, Kolter R, Losick R. 2005. A master regulator for biofilm formation by Bacillus subtilis. Mol. Microbiol. 55:739-749. http://dx.doi.org/10.1111/j.1365-2958.2004.04440.x.
    • (2005) Mol. Microbiol. , vol.55 , pp. 739-749
    • Kearns, D.B.1    Chu, F.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 9
    • 33645056701 scopus 로고    scopus 로고
    • Targets of the master regulator of biofilm formation in Bacillus subtilis
    • Chu F, Kearns DB, Branda SS, Kolter R, Losick R. 2006. Targets of the master regulator of biofilm formation in Bacillus subtilis. Mol. Microbiol. 59:1216-1228. http://dx.doi.org/10.1111/j.1365-2958.2005.05019.x.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1216-1228
    • Chu, F.1    Kearns, D.B.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 10
    • 84876256819 scopus 로고    scopus 로고
    • Molecular basis of the activity of SinR protein, the master regulator of biofilm formation in Bacillus subtilis
    • Newman JA, Rodrigues C, Lewis RJ. 2013. Molecular basis of the activity of SinR protein, the master regulator of biofilm formation in Bacillus subtilis. J. Biol. Chem. 288:10766-10778. http://dx.doi.org/10.1074/jbc.M113.455592.
    • (2013) J. Biol. Chem. , vol.288 , pp. 10766-10778
    • Newman, J.A.1    Rodrigues, C.2    Lewis, R.J.3
  • 11
    • 33645085864 scopus 로고    scopus 로고
    • A major protein component of the Bacillus subtilis biofilm matrix
    • Branda SS, Chu F, Kearns DB, Losick R, Kolter R. 2006. A major protein component of the Bacillus subtilis biofilm matrix. Mol. Microbiol. 59:1229-1238. http://dx.doi.org/10.1111/j.1365-2958.2005.05020.x.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1229-1238
    • Branda, S.S.1    Chu, F.2    Kearns, D.B.3    Losick, R.4    Kolter, R.5
  • 12
    • 0030070934 scopus 로고    scopus 로고
    • Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, SinI
    • Lewis RJ, Brannigan JA, Smith I, Wilkinson AJ. 1996. Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, SinI. FEBS Lett. 378:98-100. http://dx.doi.org/10.1016/0014-5793(95)01432-2.
    • (1996) FEBS Lett. , vol.378 , pp. 98-100
    • Lewis, R.J.1    Brannigan, J.A.2    Smith, I.3    Wilkinson, A.J.4
  • 13
    • 0032514949 scopus 로고    scopus 로고
    • An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex
    • Lewis RJ, Brannigan JA, Offen WA, Smith I, Wilkinson AJ. 1998. An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex. J. Mol. Biol. 283:907-912. http://dx.doi.org/10.1006/jmbi.1998.2163.
    • (1998) J. Mol. Biol. , vol.283 , pp. 907-912
    • Lewis, R.J.1    Brannigan, J.A.2    Offen, W.A.3    Smith, I.4    Wilkinson, A.J.5
  • 14
    • 0023973186 scopus 로고
    • Structure and expression of the Bacillus subtilis sin operon
    • Gaur NK, Cabane K, Smith I. 1988. Structure and expression of the Bacillus subtilis sin operon. J. Bacteriol. 170:1046-1053.
    • (1988) J. Bacteriol. , vol.170 , pp. 1046-1053
    • Gaur, N.K.1    Cabane, K.2    Smith, I.3
  • 15
    • 80052698341 scopus 로고    scopus 로고
    • RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y
    • Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J. 2011. RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol. Microbiol. 81:1459-1473. http://dx.doi.org/10.1111/j.1365-2958.2011.07777.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1459-1473
    • Lehnik-Habrink, M.1    Schaffer, M.2    Mäder, U.3    Diethmaier, C.4    Herzberg, C.5    Stülke, J.6
  • 16
    • 77950951089 scopus 로고    scopus 로고
    • An epigenetic switch governing daughter cell separation in Bacillus subtilis
    • Chai Y, Norman T, Kolter R, Losick R. 2010. An epigenetic switch governing daughter cell separation in Bacillus subtilis. Genes Dev. 24:754-765. http://dx.doi.org/10.1101/gad.1915010.
    • (2010) Genes Dev. , vol.24 , pp. 754-765
    • Chai, Y.1    Norman, T.2    Kolter, R.3    Losick, R.4
  • 17
    • 50049100928 scopus 로고    scopus 로고
    • SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis
    • Kobayashi K. 2008. SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis. Mol. Microbiol. 69:1399-1410. http://dx.doi.org/10.1111/j.1365-2958.2008.06369.x.
    • (2008) Mol. Microbiol. , vol.69 , pp. 1399-1410
    • Kobayashi, K.1
  • 18
    • 70449570736 scopus 로고    scopus 로고
    • Paralogous antirepressors acting on the master regulator for biofilm formation in Bacillus subtilis
    • Chai Y, Kolter R, Losick R. 2009. Paralogous antirepressors acting on the master regulator for biofilm formation in Bacillus subtilis. Mol. Microbiol. 74:876-887. http://dx.doi.org/10.1111/j.1365-2958.2009.06900.x.
    • (2009) Mol. Microbiol. , vol.74 , pp. 876-887
    • Chai, Y.1    Kolter, R.2    Losick, R.3
  • 19
    • 80055039632 scopus 로고    scopus 로고
    • A novel factor controlling bistability in Bacillus subtilis: the YmdB protein affects flagellin expression and biofilm formation
    • Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J. 2011. A novel factor controlling bistability in Bacillus subtilis: the YmdB protein affects flagellin expression and biofilm formation. J. Bacteriol. 193:5997-6007. http://dx.doi.org/10.1128/JB.05360-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 5997-6007
    • Diethmaier, C.1    Pietack, N.2    Gunka, K.3    Wrede, C.4    Lehnik-Habrink, M.5    Herzberg, C.6    Hübner, S.7    Stülke, J.8
  • 20
    • 38549172995 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of DR1281: a calcineurin-like phosphoesterase from Deinococcus radiodurans
    • Shin DH, Proudfoot M, Lim HJ, Choi IK, Yokota H, Yakunin AF, Kim R, Kim SH. 2008. Structural and enzymatic characterization of DR1281: a calcineurin-like phosphoesterase from Deinococcus radiodurans. Proteins 70:1000-1009. http://dx.doi.org/10.1002/prot.21584.
    • (2008) Proteins , vol.70 , pp. 1000-1009
    • Shin, D.H.1    Proudfoot, M.2    Lim, H.J.3    Choi, I.K.4    Yokota, H.5    Yakunin, A.F.6    Kim, R.7    Kim, S.H.8
  • 21
    • 34447569343 scopus 로고    scopus 로고
    • A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC
    • Commichau FM, Herzberg C, Tripal P, Valerius O, Stülke J. 2007. A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC. Mol. Microbiol. 65:642-654. http://dx.doi.org/10.1111/j.1365-2958.2007.05816.x.
    • (2007) Mol. Microbiol. , vol.65 , pp. 642-654
    • Commichau, F.M.1    Herzberg, C.2    Tripal, P.3    Valerius, O.4    Stülke, J.5
  • 22
    • 0003903343 scopus 로고
    • Molecular cloning: a laboratory manual, 2nd ed
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 23
    • 0031989771 scopus 로고    scopus 로고
    • Site-directed mutagenesis by combined chain reaction
    • Bi W, Stambrook PJ. 1998. Site-directed mutagenesis by combined chain reaction. Anal. Biochem. 256:137-140. http://dx.doi.org/10.1006/abio.1997.2516.
    • (1998) Anal. Biochem. , vol.256 , pp. 137-140
    • Bi, W.1    Stambrook, P.J.2
  • 24
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst F, Rapoport G. 1995. Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J. Bacteriol. 177:2403-2407.
    • (1995) J. Bacteriol. , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 25
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guérout-Fleury AM, Shazand K, Frandsen N, Stragier P. 1995. Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167:335-336. http://dx.doi.org/10.1016/0378-1119(95)00652-4.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guérout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 26
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • Wach A. 1996. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12:259-265. http://dx.doi.org/10.1002/(SICI)1097-0061(19960315)12:3259::AID-YEA9013.0.CO;2-C.
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 27
    • 1642480263 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae HPr kinase/phosphorylase
    • Merzbacher M, Detsch C, Hillen W, Stülke J. 2004. Mycoplasma pneumoniae HPr kinase/phosphorylase. Eur. J. Biochem. 271:367-374. http://dx.doi.org/10.1046/j.1432-1033.2003.03935.x.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 367-374
    • Merzbacher, M.1    Detsch, C.2    Hillen, W.3    Stülke, J.4
  • 28
    • 4344646051 scopus 로고    scopus 로고
    • The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities
    • Yakunin AF, Proudfoot M, Kuznetsova E, Savchenko A, Brown G, Arrowsmith CH, Edwards AM. 2004. The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities. J. Biol. Chem. 279:36819-36827. http://dx.doi.org/10.1074/jbc.M405120200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36819-36827
    • Yakunin, A.F.1    Proudfoot, M.2    Kuznetsova, E.3    Savchenko, A.4    Brown, G.5    Arrowsmith, C.H.6    Edwards, A.M.7
  • 29
    • 78650787467 scopus 로고    scopus 로고
    • Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2',(3')-substituted purine and pyrimidine nucleotides
    • Spangler C, Kaever V, Seifert R. 2011. Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2',(3')-substituted purine and pyrimidine nucleotides. J. Pharmacol. Exp. Ther. 336:234-241. http://dx.doi.org/10.1124/jpet.110.170993.
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 234-241
    • Spangler, C.1    Kaever, V.2    Seifert, R.3
  • 30
    • 77952580705 scopus 로고    scopus 로고
    • A liquid chromatography-coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate
    • Spangler C, Böhm A, Jenal U, Seifert R, Kaever V. 2010. A liquid chromatography-coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate. J. Microbiol. Methods 81:226-231. http://dx.doi.org/10.1016/j.mimet.2010.03.020.
    • (2010) J. Microbiol. Methods , vol.81 , pp. 226-231
    • Spangler, C.1    Böhm, A.2    Jenal, U.3    Seifert, R.4    Kaever, V.5
  • 31
    • 84872738066 scopus 로고    scopus 로고
    • Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth
    • Mehne FMP, Gunka K, Eilers H, Herzberg C, Kaever V, Stülke J. 2013. Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth. J. Biol. Chem. 288:2004-2017. http://dx.doi.org/10.1074/jbc.M112.395491.
    • (2013) J. Biol. Chem. , vol.288 , pp. 2004-2017
    • Mehne, F.M.P.1    Gunka, K.2    Eilers, H.3    Herzberg, C.4    Kaever, V.5    Stülke, J.6
  • 32
    • 76449099287 scopus 로고    scopus 로고
    • XDS. Acta Crystallogr
    • Kabsch W. 2010. XDS. Acta Crystallogr. D Biol. Crystallogr. 66:125-132. http://dx.doi.org/10.1107/S0907444909047337.
    • (2010) D Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 36
    • 0036724629 scopus 로고    scopus 로고
    • Insufficient expression of the ilv-leu operon encoding enzymes of branched-chain amino acid biosynthesis limits growth of a Bacillus subtilis ccpA mutant
    • Ludwig H, Meinken C, Matin A, Stülke J. 2002. Insufficient expression of the ilv-leu operon encoding enzymes of branched-chain amino acid biosynthesis limits growth of a Bacillus subtilis ccpA mutant. J. Bacteriol. 184:5174-5178. http://dx.doi.org/10.1128/JB.184.18.5174-5178.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 5174-5178
    • Ludwig, H.1    Meinken, C.2    Matin, A.3    Stülke, J.4
  • 37
    • 33744981623 scopus 로고    scopus 로고
    • Image processing with Image
    • Abramoff MD, Magalhaes PJ, Ram SJ. 2004. Image processing with ImageJ. Biophotonics Int. 11:36-42. http://www.imagescience.org/meijering/publications/download/bio2004.pdf.
    • (2004) J. Biophotonics Int. , vol.11 , pp. 36-42
    • Abramoff, M.D.1    Magalhaes, P.J.2    Ram, S.J.3
  • 39
    • 0041386065 scopus 로고    scopus 로고
    • UniFrag and GenomePrimer: selection of primers for genome-wide production of unique amplicons
    • van Hijum SA, de Jong A, Buist G, Kok J, Kuipers OP. 2003. UniFrag and GenomePrimer: selection of primers for genome-wide production of unique amplicons. Bioinformatics 19:1580-1582. http://dx.doi.org/10.1093/bioinformatics/btg203.
    • (2003) Bioinformatics , vol.19 , pp. 1580-1582
    • van Hijum, S.A.1    de Jong, A.2    Buist, G.3    Kok, J.4    Kuipers, O.P.5
  • 41
    • 0034948896 scopus 로고    scopus 로고
    • A Bayesian framework for the analysis of microarray expression data: regularized t-test and statistical inferences of gene changes
    • Baldi P, Long AD. 2001. A Bayesian framework for the analysis of microarray expression data: regularized t-test and statistical inferences of gene changes. Bioinformatics 17:509-519. http://dx.doi.org/10.1093/bioinformatics/17.6.509.
    • (2001) Bioinformatics , vol.17 , pp. 509-519
    • Baldi, P.1    Long, A.D.2
  • 42
    • 84862186268 scopus 로고    scopus 로고
    • SubtiWiki-a comprehensive community resource for the model organism Bacillus subtilis
    • Mäder U, Schmeisky AG, Flórez LA, Stülke J. 2012. SubtiWiki-a comprehensive community resource for the model organism Bacillus subtilis. Nucleic Acids Res. 40:D1278-D1287. http://dx.doi.org/10.1093/nar/gkr923.
    • (2012) Nucleic Acids Res. , vol.40
    • Mäder, U.1    Schmeisky, A.G.2    Flórez, L.A.3    Stülke, J.4
  • 43
    • 0033759266 scopus 로고    scopus 로고
    • Regulation of carbon catabolism in Bacillus species
    • Stülke J, Hillen W. 2000. Regulation of carbon catabolism in Bacillus species. Annu. Rev. Microbiol. 54:849-880. http://dx.doi.org/10.1146/annurev.micro.54.1.849.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 849-880
    • Stülke, J.1    Hillen, W.2
  • 44
    • 34047126471 scopus 로고    scopus 로고
    • I will survive: DNA protection in bacterial spores
    • Setlow P. 2007. I will survive: DNA protection in bacterial spores. Trends Microbiol. 15:172-180. http://dx.doi.org/10.1016/j.tim.2007.02.004.
    • (2007) Trends Microbiol. , vol.15 , pp. 172-180
    • Setlow, P.1
  • 45
    • 2942616403 scopus 로고    scopus 로고
    • Compartmentalization of gene expression during Bacillus subtilis spore formation
    • Hilbert DW, Piggot PJ. 2004. Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol. Mol. Biol. Rev. 68:234-262. http://dx.doi.org/10.1128/MMBR.68.2.234-262.2004.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 234-262
    • Hilbert, D.W.1    Piggot, P.J.2
  • 46
    • 0028116496 scopus 로고
    • Bacillus subtilis Lon protease prevents inappropriate transcription of genes under the control of sporulation transcription factor sigma G
    • Schmidt R, Decatur AL, Rather PN, Moran CP, Losick R. 1994. Bacillus subtilis Lon protease prevents inappropriate transcription of genes under the control of sporulation transcription factor sigma G. J. Bacteriol. 176:6528-6537.
    • (1994) J. Bacteriol. , vol.176 , pp. 6528-6537
    • Schmidt, R.1    Decatur, A.L.2    Rather, P.N.3    Moran, C.P.4    Losick, R.5
  • 47
    • 0027213365 scopus 로고
    • The importance of morphological events and intercellular interactions in the regulation of prespore-specific gene expression during sporulation in Bacillus subtilis
    • Partridge SR, Errington J. 1993. The importance of morphological events and intercellular interactions in the regulation of prespore-specific gene expression during sporulation in Bacillus subtilis. Mol. Microbiol. 8:945-955. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01639.x.
    • (1993) Mol. Microbiol. , vol.8 , pp. 945-955
    • Partridge, S.R.1    Errington, J.2
  • 48
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • Aravind L, Koonin EV. 1998. Phosphoesterase domains associated with DNA polymerases of diverse origins. Nucleic Acids Res. 26:3746-3752. http://dx.doi.org/10.1093/nar/26.16.3746.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 49
    • 0037083671 scopus 로고    scopus 로고
    • 3',5' cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism
    • Richter W. 2002. 3',5' cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism. Proteins 46:278-286. http://dx.doi.org/10.1002/prot.10049.
    • (2002) Proteins , vol.46 , pp. 278-286
    • Richter, W.1
  • 50
    • 57649171118 scopus 로고    scopus 로고
    • A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity
    • Keppetipola N, Shuman S. 2008. A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2',3'-cyclic nucleotide phosphodiesterase activity. J. Biol. Chem. 283:30942-30949. http://dx.doi.org/10.1074/jbc.M805064200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30942-30949
    • Keppetipola, N.1    Shuman, S.2
  • 51
    • 33751515585 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis
    • Shenoy AR, Capuder M, Draskovic P, Lamba D, Visweswariah SS, Podobnik M. 2007. Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis. J. Mol. Biol. 365:211-225. http://dx.doi.org/10.1016/j.jmb.2006.10.005.
    • (2007) J. Mol. Biol. , vol.365 , pp. 211-225
    • Shenoy, A.R.1    Capuder, M.2    Draskovic, P.3    Lamba, D.4    Visweswariah, S.S.5    Podobnik, M.6
  • 52
    • 0032915156 scopus 로고    scopus 로고
    • X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
    • Knöfel T, Strater N. 1999. X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site. Nat. Struct. Biol. 6:448-453. http://dx.doi.org/10.1038/8253.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 448-453
    • Knöfel, T.1    Strater, N.2
  • 53
    • 0035946945 scopus 로고    scopus 로고
    • Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures
    • Knöfel T, Strater N. 2001. Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures. J. Mol. Biol. 309:239-254. http://dx.doi.org/10.1006/jmbi.2001.4656.
    • (2001) J. Mol. Biol. , vol.309 , pp. 239-254
    • Knöfel, T.1    Strater, N.2
  • 54
    • 3843130769 scopus 로고    scopus 로고
    • Structural and functional characterization of a novel phosphodiesterase from Methanococcus jannaschii
    • Chen S, Yakunin AF, Kuznetsova E, Busso D, Pufan R, Proudfoot M, Kim R, Kim SH. 2004. Structural and functional characterization of a novel phosphodiesterase from Methanococcus jannaschii. J. Biol. Chem. 279:31854-31862. http://dx.doi.org/10.1074/jbc.M401059200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31854-31862
    • Chen, S.1    Yakunin, A.F.2    Kuznetsova, E.3    Busso, D.4    Pufan, R.5    Proudfoot, M.6    Kim, R.7    Kim, S.H.8
  • 55
    • 70450237641 scopus 로고    scopus 로고
    • A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability
    • Podobnik M, Tyagi R, Matange N, Dermol U, Gupta AK, Mattoo R, Seshadri K, Visweswariah SS. 2009. A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability. J. Biol. Chem. 284:32846-32857. http://dx.doi.org/10.1074/jbc.M109.049635.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32846-32857
    • Podobnik, M.1    Tyagi, R.2    Matange, N.3    Dermol, U.4    Gupta, A.K.5    Mattoo, R.6    Seshadri, K.7    Visweswariah, S.S.8
  • 56
    • 77955271184 scopus 로고    scopus 로고
    • 2',3'-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: implications for PDE screening
    • Rao F, Qi Y, Murugan E, Pasunooti S, Ji Q. 2010. 2',3'-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: implications for PDE screening. Biochem. Biophys. Res. Commun. 398:500-505. http://dx.doi.org/10.1016/j.bbrc.2010.06.107.
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 500-505
    • Rao, F.1    Qi, Y.2    Murugan, E.3    Pasunooti, S.4    Ji, Q.5
  • 57
    • 65549130634 scopus 로고    scopus 로고
    • Regulation of c-di-GMP metabolism in biofilms
    • Jonas K, Melefor O, Römling U. 2009. Regulation of c-di-GMP metabolism in biofilms. Future Microbiol. 4:341-358. http://dx.doi.org/10.2217/fmb.09.7.
    • (2009) Future Microbiol. , vol.4 , pp. 341-358
    • Jonas, K.1    Melefor, O.2    Römling, U.3
  • 58
    • 84866397780 scopus 로고    scopus 로고
    • Evidence for cyclic di-GMPmediated signaling in Bacillus subtilis
    • Chen Y, Chai Y, Guo JH, Losick R. 2012. Evidence for cyclic di-GMPmediated signaling in Bacillus subtilis. J. Bacteriol. 194:5080-5090. http://dx.doi.org/10.1128/JB.01092-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 5080-5090
    • Chen, Y.1    Chai, Y.2    Guo, J.H.3    Losick, R.4
  • 59
    • 84886035253 scopus 로고    scopus 로고
    • Functional characterization of core components of the Bacillus subtilis cyclic-di-GMP signaling pathway
    • Gao X, Mukherjee S, Matthews PM, Hammad LA, Kearns DB, Dann CE. 2013. Functional characterization of core components of the Bacillus subtilis cyclic-di-GMP signaling pathway. J. Bacteriol. 195:4782-4792. http://dx.doi.org/10.1128/JB.00373-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 4782-4792
    • Gao, X.1    Mukherjee, S.2    Matthews, P.M.3    Hammad, L.A.4    Kearns, D.B.5    Dann, C.E.6
  • 60
    • 43049087389 scopus 로고    scopus 로고
    • Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates
    • Witte G, Hartung S, Büttner K, Hopfner KP. 2008. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Mol. Cell 30:167-178. http://dx.doi.org/10.1016/j.molcel.2008.02.020.
    • (2008) Mol. Cell , vol.30 , pp. 167-178
    • Witte, G.1    Hartung, S.2    Büttner, K.3    Hopfner, K.P.4
  • 61
    • 84856048586 scopus 로고    scopus 로고
    • M in ß-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis
    • M in ß-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis. Mol. Microbiol. 83:623-639. http://dx.doi.org/10.1111/j.1365-2958.2011.07953.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 623-639
    • Luo, Y.1    Helmann, J.D.2
  • 63
    • 0021322356 scopus 로고
    • Evidence for the presence of cyclic adenosine monophosphate in Bacillus subtilis
    • Mach H, Hecker M, Mach F. 1984. Evidence for the presence of cyclic adenosine monophosphate in Bacillus subtilis. FEMS Microbiol. Lett. 22:27-30. http://dx.doi.org/10.1111/j.1574-6968.1984.tb00348.x.
    • (1984) FEMS Microbiol. Lett. , vol.22 , pp. 27-30
    • Mach, H.1    Hecker, M.2    Mach, F.3
  • 64
    • 0028364742 scopus 로고
    • Energetics of catalysis by ribonucleases: fate of the 2',3'-cyclic phosphodiester intermediate
    • Thompson JE, Venegas FD, Raines RT. 1994. Energetics of catalysis by ribonucleases: fate of the 2',3'-cyclic phosphodiester intermediate. Biochemistry 33:7408-7414. http://dx.doi.org/10.1021/bi00189a047.
    • (1994) Biochemistry , vol.33 , pp. 7408-7414
    • Thompson, J.E.1    Venegas, F.D.2    Raines, R.T.3


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