Abstract
A great diversity of bacterial cell shapes can be found in nature, suggesting that cell wall biogenesis is regulated both spatially and temporally. Although Agrobacterium tumefaciens has a rod-shaped morphology, the mechanisms underlying cell growth are strikingly different than other well-studied rod-shaped bacteria including Escherichia coli. Technological advances, such as the ability to deplete essential genes and the development of fluorescent d-amino acids, have enabled recent advances in our understanding of cell wall biogenesis during cell elongation and division of A. tumefaciens. In this review, we address how the field has evolved over the years by providing a historical overview of cell elongation and division in rod-shaped bacteria. Next, we summarize the current understanding of cell growth and cell division processes in A. tumefaciens. Finally, we highlight the need for further research to answer key questions related to the regulation of cell wall biogenesis in A. tumefaciens.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Anderson-Furgeson JC, Zupan JR, Grangeon R, Zambryski PC (2016) Loss of PodJ in Agrobacterium tumefaciens leads to ectopic polar growth, branching, and reduced cell division. J Bacteriol 198(13):1883–1891. https://doi.org/10.1128/JB.00198-16
Barner HD, Cohen SS (1956) The relation of growth to the lethal damage induced by ultraviolet irradiation in Escherichia coli. J Bacteriol 71(2):149–157
Bisson-Filho AW, Hsu YP, Squyres GR, Kuru E, Wu F, Jukes C, Sun Y, Dekker C, Holden S, VanNieuwenhze MS, Brun YV, Garner EC (2017) Treadmilling by FtsZ filaments drives peptidoglycan synthesis and bacterial cell division. Science 355(6326):739–743. https://doi.org/10.1126/science.aak9973
Bowman GR, Comolli LR, Zhu J, Eckart M, Koenig M, Downing KH, Moerner WE, Earnest T, Shapiro L (2008) A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole. Cell 134(6):945–955. https://doi.org/10.1016/j.cell.2008.07.015
Bowman GR, Comolli LR, Gaietta GM, Fero M, Hong SH, Jones Y, Lee JH, Downing KH, Ellisman MH, McAdams HH, Shapiro L (2010) Caulobacter PopZ forms a polar subdomain dictating sequential changes in pole composition and function. Mol Microbiol 76(1):173–189. https://doi.org/10.1111/j.1365-2958.2010.07088.x
Bowman GR, Perez AM, Ptacin JL, Ighodaro E, Folta-Stogniew E, Comolli LR, Shapiro L (2013) Oligomerization and higher-order assembly contribute to sub-cellular localization of a bacterial scaffold. Mol Microbiol 90(4):776–795. https://doi.org/10.1111/mmi.12398
Brown PJB, de Pedro MA, Kysela DT, Van der Henst C, Kim J, De Bolle X, Fuqua C, Brun YV (2012) Polar growth in the Alphaproteobacterial order Rhizobiales. Proc Natl Acad Sci U S A 109(5):1697–1701. https://doi.org/10.1073/pnas.1114476109
Cameron TA, Anderson-Furgeson J, Zupan JR, Zik JJ, Zambryski PC (2014) Peptidoglycan synthesis machinery in Agrobacterium tumefaciens during unipolar growth and cell division. MBio 5(3):e01219–e01214. https://doi.org/10.1128/mbio.01219-14
Cameron TA, Zupan JR, Zambryski PC (2015) The essential features and modes of bacterial polar growth. Trends Microbiol 23(6):347–353. https://doi.org/10.1016/j.tim.2015.01.003
Cava F, de Pedro MA (2014) Peptidoglycan plasticity in bacteria: emerging variability of the murein sacculus and their associated biological functions. Curr Opin Microbiol 18:46–53. https://doi.org/10.1016/j.mib.2014.01.004
Cava F, Kuru E, Brun YV, de Pedro MA (2013) Modes of cell wall growth differentiation in rod-shaped bacteria. Curr Opin Microbiol 16(6):731–737. https://doi.org/10.1016/j.mib.2013.09.004
Cho H, Wivagg CN, Kapoor M, Barry Z, Rohs PD, Suh H, Marto JA, Garner EC, Bernhardt TG (2016) Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nat Microbiol:16172. https://doi.org/10.1038/nmicrobiol.2016.172
Curtis PD, Brun YV (2014) Identification of essential alphaproteobacterial genes reveals operational variability in conserved developmental and cell cycle systems. Mol Microbiol 93(4):713–735. https://doi.org/10.1111/mmi.12686
Derouaux A, Wolf B, Fraipont C, Breukink E, Nguyen-Disteche M, Terrak M (2008) The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN. J Bacteriol 190(5):1831–1834. https://doi.org/10.1128/JB.01377-07
Du S, Lutkenhaus J (2017) Assembly and activation of the Escherichia coli divisome. Mol Microbiol 105(2):177–187. https://doi.org/10.1111/mmi.13696
Du S, Pichoff S, Lutkenhaus J (2016) FtsEX acts on FtsA to regulate divisome assembly and activity. Proc Natl Acad Sci U S A 113(34):E5052–E5061. https://doi.org/10.1073/pnas.1606656113
Ebersbach G, Briegel A, Jensen GJ, Jacobs-Wagner C (2008) A self-associating protein critical for chromosome attachment, division, and polar organization in Caulobacter. Cell 134(6):956–968. https://doi.org/10.1016/j.cell.2008.07.016
Egan AJF (2018) Bacterial outer membrane constriction. Mol Microbiol. https://doi.org/10.1111/mmi.13908
Egan AJ, Biboy J, van’t Veer I, Breukink E, Vollmer W (2015) Activities and regulation of peptidoglycan synthases. Philos Trans R Soc Lond B Biol Sci 370(1679). https://doi.org/10.1098/rstb.2015.0031
Ehrle HM, Guidry JT, Iacovetto R, Salisbury AK, Sandidge DJ, Bowman GR (2017) Polar organizing protein PopZ is required for chromosome segregation in Agrobacterium tumefaciens. J Bacteriol 199(17). https://doi.org/10.1128/jb.00111-17
Erbs G, Silipo A, Aslam S, De Castro C, Liparoti V, Flagiello A, Pucci P, Lanzetta R, Parrilli M, Molinaro A, Newman MA, Cooper RM (2008) Peptidoglycan and muropeptides from pathogens Agrobacterium and Xanthomonas elicit plant innate immunity: structure and activity. Chem Biol 15(5):438–448. https://doi.org/10.1016/j.chembiol.2008.03.017
Errington J (2015) Bacterial morphogenesis and the enigmatic MreB helix. Nat Rev Microbiol 13(4):241–248. https://doi.org/10.1038/nrmicro3398
Escobar MA, Dandekar AM (2003) Agrobacterium tumefaciens as an agent of disease. Trends Plant Sci 8(8):380–386. https://doi.org/10.1016/S1360-1385(03)00162-6
Figueroa-Cuilan W, Daniel JJ, Howell M, Sulaiman A, Brown PJB (2016) Mini-Tn7 insertion in an artificial attTn7 site enables depletion of the essential master regulator CtrA in the phytopathogen Agrobacterium tumefaciens. Appl Environ Microbiol 82(16):5015–5025. https://doi.org/10.1128/AEM.01392-16
Flärdh K (2003) Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2). Mol Microbiol 49(6):1523–1536. https://doi.org/10.1046/j.1365-2958.2003.03660.x
Flores SA, Howell M, Daniel JJ, Piccolo R, Brown PJB (2018) Absence of the Min system does not cause major cell division defects in Agrobacterium tumefaciens. Front Microbiol 9:681. https://doi.org/10.3389/fmicb.2018.00681
Fuchino K, Bagchi S, Cantlay S, Sandblad L, Wu D, Bergman J, Kamali-Moghaddam M, Flardh K, Ausmees N (2013) Dynamic gradients of an intermediate filament-like cytoskeleton are recruited by a polarity landmark during apical growth. Proc Natl Acad Sci U S A 110(21):E1889–E1897. https://doi.org/10.1073/pnas.1305358110
Fujiwara T, Fukui S (1972) Isolation of morphological mutants of Agrobacterium tumefaciens. J Bacteriol 110(2):743–746
Fujiwara T, Fukui S (1974a) Effect of D-alanine and mitomycin-C on cell morphology of Agrobacterium tumefaciens. J Gen Appl Microbiol 20(6):345–349. https://doi.org/10.2323/jgam.20.345
Fujiwara T, Fukui S (1974b) Unidirectional growth and branch formation of a morphological mutant, Agrobacterium tumefaciens. J Bacteriol 120(2):583–589
Goley ED, Comolli LR, Fero KE, Downing KH, Shapiro L (2010) DipM links peptidoglycan remodelling to outer membrane organization in Caulobacter. Mol Microbiol 77(1):56–73. https://doi.org/10.1111/j.1365-2958.2010.07222.x
Goley ED, Yeh YC, Hong SH, Fero MJ, Abeliuk E, McAdams HH, Shapiro L (2011) Assembly of the Caulobacter cell division machine. Mol Microbiol 80(6):1680–1698. https://doi.org/10.1111/j.1365-2958.2011.07677.x
Gonzalez MD, Akbay EA, Boyd D, Beckwith J (2010) Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J Bacteriol 192(11):2757–2768. https://doi.org/10.1128/JB.01609-09
Goss WA, Deitz WH, Cook TM (1964) Mechanism of action of nalidixic acid on Escherichia coli. J Bacteriol 88:1112–1118
Grangeon R, Zupan JR, Anderson-Furgeson J, Zambryski PC (2015) PopZ identifies the new pole, and PodJ identifies the old pole during polar growth in Agrobacterium tumefaciens. Proc Natl Acad Sci U S A 112(37):11666–11671. https://doi.org/10.1073/pnas.1515544112
Grangeon R, Zupan J, Jeon Y, Zambryski PC (2017) Loss of PopZ At activity in Agrobacterium tumefaciens by deletion or depletion leads to multiple growth poles, minicells, and growth defects. MBio 8(6). https://doi.org/10.1128/mbio.01881-17
Gupta R, Lavollay M, Mainardi JL, Arthur M, Bishai WR, Lamichhane G (2010) The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat Med 16(4):466–469. https://doi.org/10.1038/nm.2120
Haeusser DP, Margolin W (2016) Splitsville: structural and functional insights into the dynamic bacterial Z ring. Nat Rev Microbiol 14(5):305–319. https://doi.org/10.1038/nrmicro.2016.26
Haney SA, Glasfeld E, Hale C, Keeney D, He Z, de Boer P (2001) Genetic analysis of the Escherichia coli FtsZ.ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA. J Biol Chem 276(15):11980–11987. https://doi.org/10.1074/jbc.M009810200
Heidrich C, Ursinus A, Berger J, Schwarz H, Holtje JV (2002) Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli. J Bacteriol 184(22):6093–6099
Helmstetter CE, Pierucci O (1968) Cell division during inhibition of deoxyribonucleic acid synthesis in Escherichia coli. J Bacteriol 95(5):1627–1633
Hempel AM, Wang SB, Letek M, Gil JA, Flardh K (2008) Assemblies of DivIVA mark sites for hyphal branching and can establish new zones of cell wall growth in Streptomyces coelicolor. J Bacteriol 190(22):7579–7583. https://doi.org/10.1128/JB.00839-08
Hinz AJ, Larson DE, Smith CS, Brun YV (2003) The Caulobacter crescentus polar organelle development protein PodJ is differentially localized and is required for polar targeting of the PleC development regulator. Mol Microbiol 47(4):929–941
Holmes JA, Follett SE, Wang H, Meadows CP, Varga K, Bowman GR (2016) Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles. Proc Natl Acad Sci U S A 113(44):12490–12495. https://doi.org/10.1073/pnas.1602380113
Howell M, Brown PJB (2016) Building the bacterial cell wall at the pole. Curr Opin Microbiol 34:53–59. https://doi.org/10.1016/j.mib.2016.07.021
Howell M, Aliashkevich A, Salisbury AK, Cava F, Bowman GR, Brown PJB (2017a) Absence of the polar organizing protein PopZ results in reduced and asymmetric cell division in Agrobacterium tumefaciens. J Bacteriol 199(17). https://doi.org/10.1128/jb.00101-17
Howell M, Daniel JJ, Brown PJB (2017b) Live cell fluorescence microscopy to observe essential processes during microbial cell growth. J Vis Exp 129. https://doi.org/10.3791/56497
Huang KH, Durand-Heredia J, Janakiraman A (2013) FtsZ ring stability: of bundles, tubules, crosslinks, and curves. J Bacteriol 195(9):1859–1868. https://doi.org/10.1128/JB.02157-12
Johnson JW, Fisher JF, Mobashery S (2013) Bacterial cell-wall recycling. Ann N Y Acad Sci 1277:54–75. https://doi.org/10.1111/j.1749-6632.2012.06813.x
Kang CM, Nyayapathy S, Lee JY, Suh JW, Husson RN (2008) Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria. Microbiology 154(Pt 3):725–735. https://doi.org/10.1099/mic.0.2007/014076-0
Kilgore WW, Greenberg J (1961) Filament formation and resistane to 1-methyl-3-nitro-1-nitrosoguanidine and other radiomimetic compounds in Escherichia coli. J Bacteriol 81
Kuru E, Hughes HV, Brown PJB, Hall E, Tekkam S, Cava F, de Pedro MA, Brun YV, VanNieuwenhze MS (2012) In situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids. Angew Chem Int Ed Engl 51(50):12519–12523. https://doi.org/10.1002/anie.201206749
Kuru E, Tekkam S, Hall E, Brun YV, Van Nieuwenhze MS (2015) Synthesis of fluorescent d-amino acids and their use for probing peptidoglycan synthesis and bacterial growth in situ. Nat Protoc 10(1):33–52. https://doi.org/10.1038/nprot.2014.197
Kuykendall LD (2005) Family Rhizobiaceae. In: Brenner DJ, Krieg NR, Stanley JT, Garrity GM (eds) Bergey’s manual of systematic bacteriology, vol 2: The Proteobacteria (Part C). Springer, New York, p 324
Kysela DT, Brown PJB, Huang KC, Brun YV (2013) Biological consequences and advantages of asymmetric bacterial growth. Annu Rev Microbiol 67:417–435. https://doi.org/10.1146/annurev-micro-092412-155622
Laloux G, Jacobs-Wagner C (2013) Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization. J Cell Biol 201(6):827–841. https://doi.org/10.1083/jcb.201303036
Laloux G, Jacobs-Wagner C (2014) How do bacteria localize proteins to the cell pole? J Cell Sci 127(Pt 1):11–19. https://doi.org/10.1242/jcs.138628
Lariviere PJ, Szwedziak P, Mahone CR, Lowe J, Goley ED (2018) FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division. Mol Microbiol 107(2):180–197. https://doi.org/10.1111/mmi.13876
Latch JN, Margolin W (1997) Generation of buds, swellings, and branches instead of filaments after blocking the cell cycle of Rhizobium meliloti. J Bacteriol 179(7):2372–2381
Lavollay M, Arthur M, Fourgeaud M, Dubost L, Marie A, Veziris N, Blanot D, Gutmann L, Mainardi JL (2008) The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by l,d-transpeptidation. J Bacteriol 190(12):4360–4366. https://doi.org/10.1128/JB.00239-08
Lavollay M, Fourgeaud M, Herrmann JL, Dubost L, Marie A, Gutmann L, Arthur M, Mainardi JL (2011) The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by l,d-transpeptidases. J Bacteriol 193(3):778–782. https://doi.org/10.1128/JB.00606-10
Lea DE, Haines RB, Coulson CA (1937) The action of radiations on bacteria III—γ-rays on growing and on non-proliferating bacteria. Proc R Soc Lond B Biol Sci 123:1–21
Letek M, Fiuza M, Ordonez E, Villadangos AF, Flardh K, Mateos LM, Gil JA (2009) DivIVA uses an N-terminal conserved region and two coiled-coil domains to localize and sustain the polar growth in Corynebacterium glutamicum. FEMS Microbiol Lett 297(1):110–116. https://doi.org/10.1111/j.1574-6968.2009.01679.x
Liu B, Persons L, Lee L, de Boer PA (2015) Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli. Mol Microbiol 95(6):945–970. https://doi.org/10.1111/mmi.12906
Lutkenhaus J, Donachie WD (1979) Identification of the ftsA gene product. J Bacteriol 137(3):1088–1094
Lutkenhaus JF, Wolf-Watz H, Donachie WD (1980) Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ). J Bacteriol 142(2):615–620
Margolin W (2009) Sculpting the bacterial cell. Curr Biol 19(17):R812–R822. https://doi.org/10.1016/j.cub.2009.06.033
Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J (2006) Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol Cell 23(4):457–469. https://doi.org/10.1016/j.molcel.2006.06.019
Meeske AJ, Riley EP, Robins WP, Uehara T, Mekalanos JJ, Kahne D, Walker S, Kruse AC, Bernhardt TG, Rudner DZ (2016) SEDS proteins are a widespread family of bacterial cell wall polymerases. Nature 537(7622):634–638. https://doi.org/10.1038/nature19331
Meier EL, Razavi S, Inoue T, Goley ED (2016) A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus. Mol Microbiol 101(2):265–280. https://doi.org/10.1111/mmi.13388
Morton ER, Fuqua C (2012) Genetic manipulation of Agrobacterium. Curr Protoc Microbiol 25:3D.2.1–3D.2.15. https://doi.org/10.1002/9780471729259.mc03d02s25
Nester E (2014) Agrobacterium: nature’s genetic engineer. Front Plant Sci. https://doi.org/10.3389/fpls.2014.00730
Oliva MA, Cordell SC, Lowe J (2004) Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol 11(12):1243–1250. https://doi.org/10.1038/nsmb855
Paradis-Bleau C, Markovski M, Uehara T, Lupoli TJ, Walker S, Kahne DE, Bernhardt TG (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143(7):1110–1120. https://doi.org/10.1016/j.cell.2010.11.037
Park JT, Uehara T (2008) How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol Mol Biol Rev 72(2):211–227. https://doi.org/10.1128/MMBR.00027-07
Peters NT, Dinh T, Bernhardt TG (2011) A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators. J Bacteriol 193(18):4973–4983. https://doi.org/10.1128/JB.00316-11
Pichoff S, Lutkenhaus J (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 55(6):1722–1734. https://doi.org/10.1111/j.1365-2958.2005.04522.x
Pichoff S, Du S, Lutkenhaus J (2015) The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring. Mol Microbiol 95(6):971–987. https://doi.org/10.1111/mmi.12907
Ricard M, Hirota Y (1973) Process of cellular division in Escherichia coli: physiological study on thermosensitive mutants defective in cell division. J Bacteriol 116(1):314–322
Rolinson GN (1980) Effect of beta-lactam antibiotics on bacterial cell growth rate. J Gen Microbiol 120(2):317–323
Rowlett VW, Margolin W (2013) The bacterial Min system. Curr Biol 23(13):R553–R556. https://doi.org/10.1016/j.cub.2013.05.024
Sanders AN, Wright LF, Pavelka MS Jr (2014) Genetic characterization of mycobacterial l,d-transpeptidases. Microbiology 160(Pt 8):1795–1806. https://doi.org/10.1099/mic.0.078980-0
Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32(2):234–258. https://doi.org/10.1111/j.1574-6976.2008.00105.x
Scheffers DJ, Pinho MG (2005) Bacterial cell wall synthesis: new insights from localization studies. Microbiol Mol Biol Rev 69(4):585–607. https://doi.org/10.1128/MMBR.69.4.585-607.2005
Siegrist MS, Swarts BM, Fox DM, Lim SA, Bertozzi CR (2015) Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface. FEMS Microbiol Rev 39(2):184–202. https://doi.org/10.1093/femsre/fuu012
Tsang MJ, Bernhardt TG (2015) A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division. Mol Microbiol 95(6):925–944. https://doi.org/10.1111/mmi.12905
Typas A, Banzhaf M, van den van Saparoea Berg B, Verheul J, Biboy J, Nichols RJ, Zietek M, Beilharz K, Kannenberg K, von Rechenberg M, Breukink E, den Blaauwen T, Gross CA, Vollmer W (2010) Regulation of peptidoglycan synthesis by outer-membrane proteins. Cell 143(7):1097–1109. https://doi.org/10.1016/j.cell.2010.11.038
Typas A, Banzhaf M, Gross CA, Vollmer W (2011) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10(2):123–136. https://doi.org/10.1038/nrmicro2677
Uehara T, Bernhardt TG (2011) More than just lysins: peptidoglycan hydrolases tailor the cell wall. Curr Opin Microbiol 14(6):698–703. https://doi.org/10.1016/j.mib.2011.10.003
Uehara T, Dinh T, Bernhardt TG (2009) LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli. J Bacteriol 191(16):5094–5107. https://doi.org/10.1128/JB.00505-09
Uehara T, Parzych KR, Dinh T, Bernhardt TG (2010) Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J 29(8):1412–1422. https://doi.org/10.1038/emboj.2010.36
Van De Putte P, Van D, Roersch A (1964) The selection of mutants of Escherichia coli with impaired cell division at elevated tempratures. Mutat Res 106:121–128
van Heijenoort J (2011) Peptidoglycan hydrolases of Escherichia coli. Microbiol Mol Biol Rev 75(4):636–663. https://doi.org/10.1128/MMBR.00022-11
Viollier PH, Sternheim N, Shapiro L (2002) Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins. Proc Natl Acad Sci U S A 99(21):13831–13836. https://doi.org/10.1073/pnas.182411999
Vollmer W, Joris B, Charlier P, Foster S (2008) Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiol Rev 32(2):259–286. https://doi.org/10.1111/j.1574-6976.2007.00099.x
Weiss DS (2015) Last but not least: new insights into how FtsN triggers constriction during Escherichia coli cell division. Mol Microbiol 95(6):903–909. https://doi.org/10.1111/mmi.12925
Wu LJ, Errington J (2011) Nucleoid occlusion and bacterial cell division. Nat Rev Microbiol 10(1):8–12. https://doi.org/10.1038/nrmicro2671
Yang DC, Peters NT, Parzych KR, Uehara T, Markovski M, Bernhardt TG (2011) An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring. Proc Natl Acad Sci U S A 108(45):E1052–E1060. https://doi.org/10.1073/pnas.1107780108
Yang DC, Blair KM, Salama NR (2016) Staying in shape: the impact of cell shape on bacterial survival in diverse environments. Microbiol Mol Biol Rev 80(1):187–203. https://doi.org/10.1128/Mmbr.00031-15
Yang X, Lyu Z, Miguel A, McQuillen R, Huang KC, Xiao J (2017) GTPase activity-coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell wall synthesis. Science 355(6326):744–747. https://doi.org/10.1126/science.aak9995
Zhao G, Meier TI, Kahl SD, Gee KR, Blaszczak LC (1999) BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob Agents Chemother 43(5):1124–1128
Zupan JR, Cameron TA, Anderson-Furgeson J, Zambryski PC (2013) Dynamic FtsA and FtsZ localization and outer membrane alterations during polar growth and cell division in Agrobacterium tumefaciens. Proc Natl Acad Sci U S A 110(22):9060–9065. https://doi.org/10.1073/pnas.1307241110
Acknowledgements
Research in the Brown lab on A. tumefaciens cell growth and division is supported by the National Science Foundation (IOS1557806) and WFC is supported by a Gus T. Ridgel Fellowship. We thank Michael VanNieuwenhze (Indiana University) for the gift of the FDAA used in Fig. 2.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG, part of Springer Nature
About this chapter
Cite this chapter
Figueroa-Cuilan, W.M., Brown, P.J.B. (2018). Cell Wall Biogenesis During Elongation and Division in the Plant Pathogen Agrobacterium tumefaciens. In: Gelvin, S. (eds) Agrobacterium Biology. Current Topics in Microbiology and Immunology, vol 418. Springer, Cham. https://doi.org/10.1007/82_2018_92
Download citation
DOI: https://doi.org/10.1007/82_2018_92
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-03256-2
Online ISBN: 978-3-030-03257-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)