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Volumn 196, Issue 1, 2014, Pages 80-89

A new addition to the cell plan of anammox bacteria: "Candidatus Kuenenia stuttgartiensis" has a protein surface layer as the outermost layer of the cell

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; BACTERIAL PROTEIN; GLYCOPROTEIN; PEPTIDOGLYCAN;

EID: 84888264197     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00988-13     Document Type: Article
Times cited : (46)

References (73)
  • 3
    • 77952135313 scopus 로고    scopus 로고
    • Sewage treatment with anammox
    • Kartal B, Kuenen JG, van Loosdrecht MCM. 2010. Sewage treatment with anammox. Science 328:702-703. http://dx.doi.org/10.1126/science.1185941.
    • (2010) Science , vol.328 , pp. 702-703
    • Kartal, B.1    Kuenen, J.G.2    van Loosdrecht, M.C.M.3
  • 5
    • 78650936059 scopus 로고    scopus 로고
    • Microbial nitrogen cycling processes in oxygen minimum zones
    • Lam P, Kuypers MMM. 2011. Microbial nitrogen cycling processes in oxygen minimum zones. Annu. Rev. Mar. Sci. 3:317-345. http://dx.doi.org/10.1146/annurev-marine-120709-142814.
    • (2011) Annu. Rev. Mar. Sci. , vol.3 , pp. 317-345
    • Lam, P.1    Kuypers, M.M.M.2
  • 6
    • 81855204176 scopus 로고    scopus 로고
    • Family I. "Candidatus Brocadiaceae" fam
    • nov, In Krieg NR, Staley JT, Brown DR, Hedlund B, Paster BJ, Ward N, Ludwig W, WhitmanWB(ed), 2nd ed, Springer, New York, NY
    • Jetten MSM, Op den Camp HJM, Kuenen JG, Strous M. 2010. Family I. "Candidatus Brocadiaceae" fam. nov, p 596-602. In Krieg NR, Staley JT, Brown DR, Hedlund B, Paster BJ, Ward N, Ludwig W, WhitmanWB(ed), Bergey's manual of systematic bacteriology, 2nd ed, vol 4. Springer, New York, NY.
    • (2010) Bergey's manual of systematic bacteriology , vol.4 , pp. 596-602
    • Jetten, M.S.M.1    Op den Camp, H.J.M.2    Kuenen, J.G.3    Strous, M.4
  • 9
    • 0034937657 scopus 로고    scopus 로고
    • Cell compartmentalization in planctomycetes: novel types of structural organization for the bacterial cell
    • Lindsay MR, Webb RI, Strous M, Jetten MSM, Butler MK, Forde RJ, Fuerst JA. 2001. Cell compartmentalization in planctomycetes: novel types of structural organization for the bacterial cell. Arch. Microbiol. 175:413-429. http://dx.doi.org/10.1007/s002030100280.
    • (2001) Arch. Microbiol. , vol.175 , pp. 413-429
    • Lindsay, M.R.1    Webb, R.I.2    Strous, M.3    Jetten, M.S.M.4    Butler, M.K.5    Forde, R.J.6    Fuerst, J.A.7
  • 10
    • 62649088069 scopus 로고    scopus 로고
    • Chromatin organization and radio resistance in the bacterium Gemmata obscuriglobus
    • Lieber A, Leis A, Kushmaro A, Minsky A, Medalia O. 2009. Chromatin organization and radio resistance in the bacterium Gemmata obscuriglobus. J. Bacteriol. 191:1439-1445. http://dx.doi.org/10.1128/JB.01513-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 1439-1445
    • Lieber, A.1    Leis, A.2    Kushmaro, A.3    Minsky, A.4    Medalia, O.5
  • 11
    • 84875836360 scopus 로고    scopus 로고
    • Electron tomography of the nucleoid of Gemmata obscuriglobus reveals complex liquid crystalline cholesteric structure
    • Yee B, Sagulenko E, Morgan GP, Webb RI, Fuerst JA. 2012. Electron tomography of the nucleoid of Gemmata obscuriglobus reveals complex liquid crystalline cholesteric structure. Front. Microbiol. 3:326. http://dx.doi.org/10.3389/fmicb.2012.00326.
    • (2012) Front. Microbiol. , vol.3 , pp. 326
    • Yee, B.1    Sagulenko, E.2    Morgan, G.P.3    Webb, R.I.4    Fuerst, J.A.5
  • 12
    • 84878297375 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of bacteria with a complex endomembrane system
    • Santarella-Mellwig R, Pruggnaller S, Roos N, Mattaj IW, Devos DP. 2013. Three-dimensional reconstruction of bacteria with a complex endomembrane system. PLoS Biol. 11:e1001565. http://dx.doi.org/10.1371/journal.pbio.1001565.
    • (2013) PLoS Biol. , vol.11
    • Santarella-Mellwig, R.1    Pruggnaller, S.2    Roos, N.3    Mattaj, I.W.4    Devos, D.P.5
  • 13
    • 84875776503 scopus 로고    scopus 로고
    • Genomic analysis indicates the presence of an asymmetric bilayer outer membrane in Planctomycetes and Verrucomicrobia
    • Speth DR, van Teeseling MCF, Jetten MSM. 2012. Genomic analysis indicates the presence of an asymmetric bilayer outer membrane in Planctomycetes and Verrucomicrobia. Front. Microbiol. 3:304. http://dx.doi.org/10.3389/fmicb.2012.00304.
    • (2012) Front. Microbiol. , vol.3 , pp. 304
    • Speth, D.R.1    van Teeseling, M.C.F.2    Jetten, M.S.M.3
  • 15
    • 84876810172 scopus 로고    scopus 로고
    • The anammoxosome organelle is crucial for the energy metabolism of anaerobic ammonium oxidizing bacteria
    • van Teeseling MCF, Neumann S, van Niftrik L. 2013. The anammoxosome organelle is crucial for the energy metabolism of anaerobic ammonium oxidizing bacteria. J. Mol. Microbiol. Biotechnol. 23:104-117. http://dx.doi.org/10.1159/000346547.
    • (2013) J. Mol. Microbiol. Biotechnol. , vol.23 , pp. 104-117
    • van Teeseling, M.C.F.1    Neumann, S.2    van Niftrik, L.3
  • 18
    • 0021139615 scopus 로고
    • Cell wall studies on budding bacteria of the Planctomycetes/Pasteuria group and on a Prosthecomicrobium sp
    • König E, Schlesner H, Hirsch P. 1984. Cell wall studies on budding bacteria of the Planctomycetes/Pasteuria group and on a Prosthecomicrobium sp. Arch. Microbiol. 138:200-205. http://dx.doi.org/10.1007/BF00402120.
    • (1984) Arch. Microbiol. , vol.138 , pp. 200-205
    • König, E.1    Schlesner, H.2    Hirsch, P.3
  • 19
    • 0022474094 scopus 로고
    • Chemical composition of the peptidoglycan-free cell envelopes of budding bacteria of the Pirella/Planctomycetes group
    • Liesack W, König H, Schlesner H, Hirsch P. 1986. Chemical composition of the peptidoglycan-free cell envelopes of budding bacteria of the Pirella/Planctomycetes group. Arch. Microbiol. 145:361-366. http://dx.doi.org/10.1007/BF00470872.
    • (1986) Arch. Microbiol. , vol.145 , pp. 361-366
    • Liesack, W.1    König, H.2    Schlesner, H.3    Hirsch, P.4
  • 20
    • 84930027427 scopus 로고    scopus 로고
    • Cell biology of anaerobic ammonium-oxidizing bacteria: unique prokaryotes with an energy- conserving intracellular compartment, p 89-123
    • In Fuerst JA (ed), Planctomycetes, cell structure, origins and biology, Springer, Humana Press, New York, NY
    • Neumann S, van Teeseling MCF, van Niftrik L. 2013. Cell biology of anaerobic ammonium-oxidizing bacteria: unique prokaryotes with an energy- conserving intracellular compartment, p 89-123. In Fuerst JA (ed), Planctomycetes: cell structure, origins and biology. Springer, Humana Press, New York, NY.
    • (2013)
    • Neumann, S.1    van Teeseling, M.C.F.2    van Niftrik, L.3
  • 21
    • 0035018011 scopus 로고    scopus 로고
    • Formation of the glycan chains in the synthesis of bacterial peptidoglycan
    • van Heijenoort J. 2001. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11:25R-36R. http://dx.doi.org/10.1093/glycob/11.3.25R.
    • (2001) Glycobiology , vol.11
    • van Heijenoort, J.1
  • 24
    • 35148889967 scopus 로고    scopus 로고
    • Proteinaceous surface layers of Archaea: ultrastructure and biochemistry, p 315-340
    • In Cavicchioli R (ed), Archaea: molecular and cell biology. ASM Press, Washington, DC
    • König H, Rachel R, Claus H. 2007. Proteinaceous surface layers of Archaea: ultrastructure and biochemistry, p 315-340. In Cavicchioli R (ed), Archaea: molecular and cell biology. ASM Press, Washington, DC.
    • (2007)
    • König, H.1    Rachel, R.2    Claus, H.3
  • 25
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: structurefunction relationships and their biotechnological applications
    • Sleytr UB, Sára M. 1997. Bacterial and archaeal S-layer proteins: structurefunction relationships and their biotechnological applications. Trends Biotechnol. 15:20-26. http://dx.doi.org/10.1016/S0167-7799(96)10063-9.
    • (1997) Trends Biotechnol. , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sára, M.2
  • 26
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layer research: an overview
    • Sleytr UB. 1997. Basic and applied S-layer research: an overview. FEMS Microbiol. Rev. 20:5-12. http://dx.doi.org/10.1016/S0168-6445(97)00039-9.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 27
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper M, Berg E, Mengele R, Strobel I. 1990. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J. Bacteriol. 172: 7111-7118.
    • (1990) J. Bacteriol. , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 28
    • 0035258293 scopus 로고    scopus 로고
    • Prokaryotic glycosylation
    • Schäffer C, Graninger M, Messner P. 2001. Prokaryotic glycosylation. Proteomics 1:248-261. http://dx.doi.org/10.1002/1615-9861(200102)1:2248::AID -PROT248 3.0.CO;2-K.
    • (2001) Proteomics , vol.1 , pp. 248-261
    • Schäffer, C.1    Graninger, M.2    Messner, P.3
  • 29
    • 15844394070 scopus 로고    scopus 로고
    • The structure of secondary cell wall polymers: how Gram-positive bacteria stick their cell walls together
    • Schäffer C, Messner P. 2005. The structure of secondary cell wall polymers: how Gram-positive bacteria stick their cell walls together. Microbiology 151:643-651. http://dx.doi.org/10.1099/mic.0.27749-0.
    • (2005) Microbiology , vol.151 , pp. 643-651
    • Schäffer, C.1    Messner, P.2
  • 30
    • 0034283014 scopus 로고    scopus 로고
    • Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation
    • Mesnage S, Fontaine T, Mignot T, Delpierre M, Mock M, Fouet A. 2000. Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J. 19:4473-4484. http://dx.doi.org/10.1093/emboj/19.17.4473.
    • (2000) EMBO J. , vol.19 , pp. 4473-4484
    • Mesnage, S.1    Fontaine, T.2    Mignot, T.3    Delpierre, M.4    Mock, M.5    Fouet, A.6
  • 31
    • 0035253107 scopus 로고    scopus 로고
    • Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Grampositive bacteria
    • Sára M. 2001. Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Grampositive bacteria. Trends Microbiol. 9:47-49. http://dx.doi.org/10.1016/S0966-842X(00)01905-3.
    • (2001) Trends Microbiol. , vol.9 , pp. 47-49
    • Sára, M.1
  • 32
    • 0032464347 scopus 로고    scopus 로고
    • Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions
    • Engelhardt H, Peters J. 1998. Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions. J. Struct. Biol. 124:276-302. http://dx.doi.org/10.1006/jsbi.1998.4070.
    • (1998) J. Struct. Biol. , vol.124 , pp. 276-302
    • Engelhardt, H.1    Peters, J.2
  • 33
    • 84855870250 scopus 로고    scopus 로고
    • Archaeosortase and exosortases are widely distributed systems linking membrane transit with posttranslation modifications
    • Haft DH, Payne SH, Selengut JD. 2012. Archaeosortase and exosortases are widely distributed systems linking membrane transit with posttranslation modifications. J. Bacteriol. 194:36-48. http://dx.doi.org/10.1128/JB.06026-11.
    • (2012) J. Bacteriol. , vol.194 , pp. 36-48
    • Haft, D.H.1    Payne, S.H.2    Selengut, J.D.3
  • 35
    • 78650933583 scopus 로고    scopus 로고
    • Cultivation, detection, and ecophysiology of anaerobic ammonium-oxidizing bacteria, p 89-108
    • In Klotz MG (ed), Methods in enzymology, Academic Press, San Diego, CA
    • Kartal B, Geerts W, Jetten MSM. 2011. Cultivation, detection, and ecophysiology of anaerobic ammonium-oxidizing bacteria, p 89-108. In Klotz MG (ed), Methods in enzymology, vol 486. Academic Press, San Diego, CA.
    • (2011) , pp. 486
    • Kartal, B.1    Geerts, W.2    Jetten, M.S.M.3
  • 38
    • 0029945635 scopus 로고    scopus 로고
    • Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system
    • Saxton WO. 1996. Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system. J. Struct. Biol. 116:230-236. http://dx.doi.org/10.1006/jsbi.1996.0035.
    • (1996) J. Struct. Biol. , vol.116 , pp. 230-236
    • Saxton, W.O.1
  • 39
    • 0002484511 scopus 로고
    • Correlation averaging and 3-D reconstruction of 2d crystalline membranes and macromolecules, p 357-413
    • In Mayer F (ed), Methods in microbiology, Academic Press, London, United Kingdom
    • Engelhardt H. 1988. Correlation averaging and 3-D reconstruction of 2d crystalline membranes and macromolecules, p 357-413. In Mayer F (ed), Methods in microbiology, vol 20. Academic Press, London, United Kingdom.
    • (1988) , vol.20
    • Engelhardt, H.1
  • 40
    • 0029036578 scopus 로고
    • Reconstruction and representation of surface data from two-dimensional crystalline, biological macromolecules
    • Fuchs KH, Tittmann P, Krusche K, Gross H. 1995. Reconstruction and representation of surface data from two-dimensional crystalline, biological macromolecules. Bioimaging 3:12-24. http://dx.doi.org/10.1002/1361-6374(199503)3:112::AID-BIO2 3.3.CO;2-U.
    • (1995) Bioimaging , vol.3 , pp. 12-24
    • Fuchs, K.H.1    Tittmann, P.2    Krusche, K.3    Gross, H.4
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 15:680-685.
    • (1970) Nature , vol.15 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 30344463700 scopus 로고
    • Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate
    • In Ginsburg V (ed), Academic Press, San Diego, CA.
    • Segrest JP, Jackson RL. 1972. Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, p 54-63. In Ginsburg V (ed), Methods in enzymology, vol 28. Academic Press, San Diego, CA.
    • (1972) Methods in enzymology , vol.28 , pp. 54-63
    • Segrest, J.P.1    Jackson, R.L.2
  • 43
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
    • Nielsen ML, Vermeulen M, Bonaldi T, Cox J, Moroder L, Man M. 2008. Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods 5:459-460. http://dx.doi.org/10.1038/nmeth0608-459.
    • (2008) Nat. Methods , vol.5 , pp. 459-460
    • Nielsen, M.L.1    Vermeulen, M.2    Bonaldi, T.3    Cox, J.4    Moroder, L.5    Man, M.6
  • 46
    • 34247323554 scopus 로고    scopus 로고
    • Immunogold labeling of cryosections from high-pressure frozen cells
    • van Donselaar E, Posthuma G, Zeuschner D, Humbel BM, Slot JW. 2007. Immunogold labeling of cryosections from high-pressure frozen cells. Traffic 8:471-485. http://dx.doi.org/10.1111/j.1600-0854.2007.00552.x.
    • (2007) Traffic , vol.8 , pp. 471-485
    • van Donselaar, E.1    Posthuma, G.2    Zeuschner, D.3    Humbel, B.M.4    Slot, J.W.5
  • 47
    • 0021693911 scopus 로고
    • Surface reliefs derived from heavy-metalshadowed specimens-Fourier space techniques applied to periodic objects
    • Guckenberger R. 1985. Surface reliefs derived from heavy-metalshadowed specimens-Fourier space techniques applied to periodic objects. Ultramicroscopy 16:357-370. http://dx.doi.org/10.1016/0304-3991(85)90104-4.
    • (1985) Ultramicroscopy , vol.16 , pp. 357-370
    • Guckenberger, R.1
  • 48
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H. 2011. SignalP 40: discriminating signal peptides from transmembrane regions. Nat. Methods 8:785-786. http://dx.doi.org/10.1038/nmeth.1701.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 50
    • 3242876311 scopus 로고    scopus 로고
    • BLAST: at the core of a powerful and diverse set of sequence analysis tools
    • McGinnis S, Madden TL. 2004. BLAST: at the core of a powerful and diverse set of sequence analysis tools. Nucleic Acids Res. 32:W20-W25. http://dx.doi.org/10.1093/nar/gkh435.
    • (2004) Nucleic Acids Res. , vol.32
    • McGinnis, S.1    Madden, T.L.2
  • 52
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Söding J. 2005. Protein homology detection by HMM-HMM comparison. Bioinformatics 21:951-960. http://dx.doi.org/10.1093/bioinformatics/bti125.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 53
    • 74249104499 scopus 로고    scopus 로고
    • Fast and accurate automatic structure prediction with HHpred
    • Hildebrand A, Remmert M, Biegert A, Södling J. 2009. Fast and accurate automatic structure prediction with HHpred. Proteins 77(Suppl 9):128-132. http://dx.doi.org/10.1002/prot.22499.
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 128-132
    • Hildebrand, A.1    Remmert, M.2    Biegert, A.3    Södling, J.4
  • 55
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer ELL. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580. http://dx.doi.org/10.1006/jmbi.2000.4315.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.L.4
  • 56
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • In Glasgow J, Littlejohn T, Major F, Lathrop R, SankoffD, Sensen C (ed), Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology. AAAI Press, Menlo Park, CA.
    • Sonnhammer ELL, von Heijne G, Krogh A. 1998. A hidden Markov model for predicting transmembrane helices in protein sequences, p 175-182. In Glasgow J, Littlejohn T, Major F, Lathrop R, SankoffD, Sensen C (ed), Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology. AAAI Press, Menlo Park, CA.
    • (1998) , pp. 175-182
    • Sonnhammer, E.L.L.1    von Heijne, G.2    Krogh, A.3
  • 57
    • 0024456474 scopus 로고
    • Structure, surface charge, and selfassembly of the S-layer lattice from Bacillus coagulans E38-66
    • Pum D, Sára M, Sleytr UB. 1989. Structure, surface charge, and selfassembly of the S-layer lattice from Bacillus coagulans E38-66. J. Bacteriol. 171:5296-5303.
    • (1989) J. Bacteriol. , vol.171 , pp. 5296-5303
    • Pum, D.1    Sára, M.2    Sleytr, U.B.3
  • 58
    • 82355169822 scopus 로고    scopus 로고
    • Analysis of the surface proteins of Acidithiobacillus ferrooxidans strain SP5/1 and the new, pyrite-oxidizing Acidithiobacillus isolate HV2/2, and their possible involvement in pyrite oxidation
    • Klingl A, Moissl-Eichinger C, Wanner G, Zweck J, Huber H, Thomm M, Rachel R. 2011. Analysis of the surface proteins of Acidithiobacillus ferrooxidans strain SP5/1 and the new, pyrite-oxidizing Acidithiobacillus isolate HV2/2, and their possible involvement in pyrite oxidation. Arch. Microbiol. 193:867-882. http://dx.doi.org/10.1007/s00203-011-0720-y.
    • (2011) Arch. Microbiol. , vol.193 , pp. 867-882
    • Klingl, A.1    Moissl-Eichinger, C.2    Wanner, G.3    Zweck, J.4    Huber, H.5    Thomm, M.6    Rachel, R.7
  • 59
    • 84863611053 scopus 로고    scopus 로고
    • GlycoPP: a webserver for prediction of N- and O-glycosites in prokaryotic protein sequences
    • Chauhan JS, Bhat AH, Raghava GPS, Rao A. 2012. GlycoPP: a webserver for prediction of N- and O-glycosites in prokaryotic protein sequences. PLoS One 7:e40155. http://dx.doi.org/10.1371/journal.pone.0040155.
    • (2012) PLoS One , vol.7
    • Chauhan, J.S.1    Bhat, A.H.2    Raghava, G.P.S.3    Rao, A.4
  • 61
    • 70349392087 scopus 로고    scopus 로고
    • Prokaryotic protein glycosylation is rapidly expanding from "curiosity" to "ubiquity"
    • Messner P. 2009. Prokaryotic protein glycosylation is rapidly expanding from "curiosity" to "ubiquity." Chembiochem 10:2151-2154. http://dx.doi.org/10.1002/cbic.200900388.
    • (2009) Chembiochem , vol.10 , pp. 2151-2154
    • Messner, P.1
  • 62
    • 0034965222 scopus 로고    scopus 로고
    • Identification of lipopolysaccharide O antigen synthesis genes required for attachment of the S-layer of Caulobacter crescentus
    • Awram P, Smit J. 2001. Identification of lipopolysaccharide O antigen synthesis genes required for attachment of the S-layer of Caulobacter crescentus. Microbiology 147:1451-1460. http://mic.sgmjournals.org/content/147/6/1451.long.
    • (2001) Microbiology , vol.147 , pp. 1451-1460
    • Awram, P.1    Smit, J.2
  • 63
    • 0028946548 scopus 로고
    • A lipopolysaccharidebinding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs
    • Dworkin J, Tummuru MK, Blaser MJ. 1995. A lipopolysaccharidebinding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs. J. Bacteriol. 177:1734-1741.
    • (1995) J. Bacteriol. , vol.177 , pp. 1734-1741
    • Dworkin, J.1    Tummuru, M.K.2    Blaser, M.J.3
  • 64
    • 35148873213 scopus 로고    scopus 로고
    • Are S-layers exoskeletons? The basic function of protein surface layer revisited
    • Engelhardt H. 2007. Are S-layers exoskeletons? The basic function of protein surface layer revisited. J. Struct. Biol. 160:115-124. http://dx.doi.org/10.1016/j.jsb.2007.08.003.
    • (2007) J. Struct. Biol. , vol.160 , pp. 115-124
    • Engelhardt, H.1
  • 65
    • 0033984760 scopus 로고    scopus 로고
    • S-layer proteins
    • Sára M, Sleytr UB. 2000. S-layer proteins. J. Bacteriol. 182:859-868. http://dx.doi.org/10.1128/JB.182.4.859-868.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 859-868
    • Sára, M.1    Sleytr, U.B.2
  • 66
    • 84874105332 scopus 로고    scopus 로고
    • Characterization of a S-layer protein from Lactobacillus crispatus K313 and the domains responsible for binding to cell wall and adherence to collagen
    • Sun Z, Kong J, Hu S, Kong W, Lu W, Liu W. 2013. Characterization of a S-layer protein from Lactobacillus crispatus K313 and the domains responsible for binding to cell wall and adherence to collagen. Appl. Microbiol. Biotechnol. 97:1941-1952. http://dx.doi.org/10.1007/s00253-012-4044-x.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 1941-1952
    • Sun, Z.1    Kong, J.2    Hu, S.3    Kong, W.4    Lu, W.5    Liu, W.6
  • 67
    • 0022981601 scopus 로고
    • 16S ribosomal RNAand cell wall analysis of Gemmata obscuriglobus, a new member of the order Planctomycetales
    • Stackebrandt E, Wehmeyer U, Liesack W. 1986. 16S ribosomal RNAand cell wall analysis of Gemmata obscuriglobus, a new member of the order Planctomycetales. FEMS Microbiol. Lett. 37:289-292. http://dx.doi.org/10.1111/j.1574-6968.1986.tb01810.x.
    • (1986) FEMS Microbiol. Lett. , vol.37 , pp. 289-292
    • Stackebrandt, E.1    Wehmeyer, U.2    Liesack, W.3
  • 68
    • 67650494990 scopus 로고    scopus 로고
    • Involvement of cell surface structures in size-independent grazing resistance of freshwater Actinobacteria
    • Tarao M, Jezbera J, Hahn MW. 2009. Involvement of cell surface structures in size-independent grazing resistance of freshwater Actinobacteria. Appl. Environ. Microbiol. 75:4720-4726. http://dx.doi.org/10.1128/AEM.00251-09.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4720-4726
    • Tarao, M.1    Jezbera, J.2    Hahn, M.W.3
  • 69
    • 84876259504 scopus 로고    scopus 로고
    • To invade or not to invade: two approaches to a prokaryotic predatory life cycle
    • Chanyi RM, Ward C, Pechey A, Koval SF. 2013. To invade or not to invade: two approaches to a prokaryotic predatory life cycle. Can. J. Microbiol. 59:273-279. http://dx.doi.org/10.1139/cjm-2013-0041.
    • (2013) Can. J. Microbiol. , vol.59 , pp. 273-279
    • Chanyi, R.M.1    Ward, C.2    Pechey, A.3    Koval, S.F.4
  • 70
    • 0028907616 scopus 로고
    • The S-layer from Bacillus stearothermophilus DSM 2358 functions as an adhesion site for a high-molecular-weight amylase
    • Egelseer E, Schocher I, Sára M, Sleytr UB. 1995. The S-layer from Bacillus stearothermophilus DSM 2358 functions as an adhesion site for a high-molecular-weight amylase. J. Bacteriol. 177:1444-1451.
    • (1995) J. Bacteriol. , vol.177 , pp. 1444-1451
    • Egelseer, E.1    Schocher, I.2    Sára, M.3    Sleytr, U.B.4
  • 71
    • 35148893696 scopus 로고    scopus 로고
    • Mechanism of osmoprotection by archaeal S-layers: a theoretical study
    • Engelhardt H. 2007. Mechanism of osmoprotection by archaeal S-layers: a theoretical study. J. Struct. Biol. 160:190-199.
    • (2007) J. Struct. Biol. , vol.160 , pp. 190-199
    • Engelhardt, H.1
  • 72
    • 79956100429 scopus 로고    scopus 로고
    • The archaeal cell envelope
    • Albers S-V, Meyer BH. 2011. The archaeal cell envelope. Nat. Rev. Microbiol. 9:414-426. http://dx.doi.org/10.1038/nrmicro2576.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 414-426
    • Albers, S.-V.1    Meyer, B.H.2
  • 73
    • 0031831035 scopus 로고    scopus 로고
    • The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded -sheet proteins by its sequence and properties
    • Baldermann C, Lupas A, Lubieniecki J, Engelhardt H. 1998. The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded -sheet proteins by its sequence and properties. J. Bacteriol. 180:3741-3749.
    • (1998) J. Bacteriol. , vol.180 , pp. 3741-3749
    • Baldermann, C.1    Lupas, A.2    Lubieniecki, J.3    Engelhardt, H.4


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