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Protein Targeting during Sporulation

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  • Author: Jonathan Dworkin1
  • Editors: Patrick Eichenberger2, Adam Driks3
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    Affiliations: 1: Department of Microbiology & Immunology, College of Physicians and Surgeons, Columbia University, New York, NY 10032; 2: New York University, New York, NY; 3: Loyola University Medical Center, Maywood, IL
  • Source: microbiolspec February 2014 vol. 2 no. 1 doi:10.1128/microbiolspec.TBS-0006-2012
  • Received 09 September 2012 Accepted 04 April 2013 Published 14 February 2014
  • J. Dworkin, jonathan.dworkin@columbia.edu
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  • Abstract:

    The Gram-positive bacterium initiates the formation of an endospore in response to conditions of nutrient limitation. The morphological differentiation that spores undergo initiates with the formation of an asymmetric septum near to one pole of the cell, forming a smaller compartment, the forespore, and a larger compartment, the mother cell. This process continues with the complex morphogenesis of the spore as governed by an intricate series of interactions between forespore and mother cell proteins across the inner and outer forespore membranes. Given that these interactions occur at a particular place in the cell, a critical question is how the proteins involved in these processes get properly targeted, and we discuss recent progress in identifying mechanisms responsible for this targeting.

  • Citation: Dworkin J. 2014. Protein Targeting during Sporulation. Microbiol Spectrum 2(1):TBS-0006-2012. doi:10.1128/microbiolspec.TBS-0006-2012.

Key Concept Ranking

Integral Membrane Proteins
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Peripheral Membrane Proteins
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Outer Membrane Proteins
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References

1. Cohn F. 1876. Untersuchungen ueber Bakterien. IV. Beitraege zur Biologie der Bacillen. Beitr Biol Planz 2:249–276.
2. Koch R. 1876. Die Ätiologie der Milzbrand-Krankheit, begründet auf die Entwicklungsgeschichte des Bacillus anthracis. Beitr Biol Pflanz 2:277–231.
3. Spitzer J. 2011. From water and ions to crowded biomacromolecules: in vivo structuring of a prokaryotic cell. Microbiol Mol Biol Rev 75:491–506. [PubMed][CrossRef]
4. Errington J. 2003. Regulation of endospore formation in Bacillus subtilis. Nat Rev Microbiol 1:117–126. [PubMed][CrossRef]
5. Hilbert DW, Piggot PJ. 2004. Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol Mol Biol Rev 68:234–262. [PubMed][CrossRef]
6. Kroos L. 2007. The Bacillus and Myxococcus developmental networks and their transcriptional regulators. Annu Rev Genet 41:13–39. [PubMed][CrossRef]
7. Higgins D, Dworkin J. 2012. Recent progress in Bacillus subtilis sporulation. FEMS Microbiol Rev 36:131–148. [PubMed][CrossRef]
8. Swulius MT, Jensen GJ. 2012. The helical MreB cytoskeleton in Escherichia coli MC1000/pLE7 is an artifact of the N-terminal yellow fluorescent protein tag. J Bacteriol 194:6382–6386. [PubMed][CrossRef]
9. Landgraf D, Okumus B, Chien P, Baker TA, Paulsson J. 2012. Segregation of molecules at cell division reveals native protein localization. Nat Methods 9:480–482. [PubMed][CrossRef]
10. Veening JW, Stewart EJ, Berngruber TW, Taddei F, Kuipers OP, Hamoen LW. 2008. Bet-hedging and epigenetic inheritance in bacterial cell development. Proc Natl Acad Sci USA 105:4393–4398. [PubMed][CrossRef]
11. Bi EF, Lutkenhaus J. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature 354:161–164. [CrossRef]
12. Li Z, Trimble MJ, Brun YV, Jensen GJ. 2007. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 26:4694–4708. [PubMed][CrossRef]
13. Michie KA, Monahan LG, Beech PL, Harry EJ. 2006. Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ. J Bacteriol 188:1680–1690. [PubMed][CrossRef]
14. Osawa M, Anderson DE, Erickson HP. 2008. Reconstitution of contractile FtsZ rings in liposomes. Science 320:792–794. [PubMed][CrossRef]
15. Allard JF, Cytrynbaum EN. 2009. Force generation by a dynamic Z-ring in Escherichia coli cell division. Proc Natl Acad Sci USA 106:145–150. [PubMed][CrossRef]
16. Lan G, Daniels BR, Dobrowsky TM, Wirtz D, Sun SX. 2009. Condensation of FtsZ filaments can drive bacterial cell division. Proc Natl Acad Sci USA 106:121–126. [PubMed][CrossRef]
17. Levin PA, Losick R. 1996. Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis. Genes Dev 10:478–488. [PubMed]
18. Lowe J, Amos LA. 1998. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391:203–206. [PubMed][CrossRef]
19. Ben-Yehuda S, Losick R. 2002. Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ. Cell 109:257–266. [PubMed]
20. Wagner-Herman JK, Bernard R, Dunne R, Bisson-Filho AW, Kumar K, Nguyen T, Mulcahy L, Koullias J, Gueiros-Filho FJ, Rudner DZ. 2012. RefZ facilitates the switch from medial to polar division during spore formation in Bacillus subtilis. J Bacteriol 194:4608–4618. [PubMed][CrossRef]
21. Young IE. 1964. Characteristics of an abortively disporic variant of Bacillus cereus. J Bacteriol 88:242–254. [PubMed]
22. Dworkin J. 2009. Cellular polarity in prokaryotic organisms. Cold Spring Harbor Perspect Biol 1:a003368. [PubMed][CrossRef]
23. Chary VK, Hilbert DW, Higgins ML, Piggot PJ. 2000. The putative DNA translocase SpoIIIE is required for sporulation of the symmetrically dividing coccal species Sporosarcina ureae. Mol Microbiol 35:612–622. [PubMed]
24. Pogliano J, Osborne N, Sharp MD, Abanes-De Mello A, Perez A, Sun YL, Pogliano K. 1999. A vital stain for studying membrane dynamics in bacteria: a novel mechanism controlling septation during Bacillus subtilis sporulation. Mol Microbiol 31:1149–1159. [PubMed]
25. Eichenberger P, Fawcett P, Losick R. 2001. A three-protein inhibitor of polar septation during sporulation in Bacillus subtilis. Mol Microbiol 42:1147–1162. [PubMed]
26. Dworkin J. 2003. Transient genetic asymmetry and cell fate in a bacterium. Trends Genet 19:107–112. [PubMed][CrossRef]
27. Dworkin J, Losick R. 2001. Differential gene expression governed by chromosomal spatial asymmetry. Cell 107:339–346. [PubMed]
28. Khvorova A, Chary VK, Hilbert DW, Piggot PJ. 2000. The chromosomal location of the Bacillus subtilis sporulation gene spoIIR is important for its function. J Bacteriol 182:4425–4429. [PubMed]
29. Ben-Yehuda S, Rudner DZ, Losick R. 2003. RacA, a bacterial protein that anchors chromosomes to the cell poles. Science 299:532–536. [PubMed][CrossRef]
30. Wu LJ, Errington J. 2003. RacA and the Soj-Spo0J system combine to effect polar chromosome segregation in sporulating Bacillus subtilis. Mol Microbiol 49:1463–1475. [PubMed]
31. Lenarcic R, Halbedel S, Visser L, Shaw M, Wu LJ, Errington J, Marenduzzo D, Hamoen LW. 2009. Localisation of DivIVA by targeting to negatively curved membranes. EMBO J 28:2272–2282. [PubMed][CrossRef]
32. Adams DW, Errington J. 2009. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat Rev Microbiol 7:642–653. [PubMed][CrossRef]
33. Goehring NW, Beckwith J. 2005. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 15:R514–R526. [PubMed][CrossRef]
34. Lucet I, Feucht A, Yudkin MD, Errington J. 2000. Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE. EMBO J 19:1467–1475. [PubMed][CrossRef]
35. King N, Dreesen O, Stragier P, Pogliano K, Losick R. 1999. Septation, dephosphorylation, and the activation of sigmaF during sporulation in Bacillus subtilis. Genes Dev 13:1156–1167. [PubMed]
36. Levin PA, Losick R, Stragier P, Arigoni F. 1997. Localization of the sporulation protein SpoIIE in Bacillus subtilis is dependent upon the cell division protein FtsZ. Mol Microbiol 25:839–846. [PubMed]
37. Barak I, Behari J, Olmedo G, Guzman P, Brown DP, Castro E, Walker D, Westpheling J, Youngman P. 1996. Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly. Mol Microbiol 19:1047–1060. [PubMed]
38. Barak I, Youngman P. 1996. SpoIIE mutants of Bacillus subtilis comprise two distinct phenotypic classes consistent with a dual functional role for the SpoIIE protein. J Bacteriol 178:4984–4989. [PubMed]
39. Losick R, Stragier P. 1992. Crisscross regulation of cell-type-specific gene expression during development in B. subtilis. Nature 355:601–604. [PubMed][CrossRef]
40. Duncan L, Alper S, Arigoni F, Losick R, Stragier P. 1995. Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division. Science 270:641–644. [PubMed]
41. Arigoni F, Pogliano K, Webb CD, Stragier P, Losick R. 1995. Localization of protein implicated in establishment of cell type to sites of asymmetric division. Science 270:637–640. [PubMed]
42. Guberman JM, Fay A, Dworkin J, Wingreen NS, Gitai Z. 2008. PSICIC: noise and asymmetry in bacterial division revealed by computational image analysis at sub-pixel resolution. PLoS Comput Biol 4:e1000233. doi:10.1371/journal.pcbi.1000233. [PubMed][CrossRef]
43. Burton B, Dubnau D. 2010. Membrane-associated DNA transport machines. Cold Spring Harbor Perspect Biol 2:a000406. doi:10.1101/cshperspect.a000406. [PubMed][CrossRef]
44. Fiche JB, Cattoni DI, Diekmann N, Langerak JM, Clerte C, Royer CA, Margeat E, Doan T, Nollmann M. 2013. Recruitment, assembly, and molecular architecture of the SpoIIIE DNA pump revealed by superresolution microscopy. PLoS Biol 11:e1001557. doi:10.1371/journal.pbio.1001557. [PubMed][CrossRef]
45. Wu LJ, Errington J. 1997. Septal localization of the SpoIIIE chromosome partitioning protein in Bacillus subtilis. EMBO J 16:2161–2169. [PubMed][CrossRef]
46. Ben-Yehuda S, Rudner DZ, Losick R. 2003. Assembly of the SpoIIIE DNA translocase depends on chromosome trapping in Bacillus subtilis. Curr Biol 13:2196–2200. [PubMed]
47. Becker EC, Pogliano K. 2007. Cell-specific SpoIIIE assembly and DNA translocation polarity are dictated by chromosome orientation. Mol Microbiol 66:1066–1079. [PubMed][CrossRef]
48. Ptacin JL, Nollmann M, Becker EC, Cozzarelli NR, Pogliano K, Bustamante C. 2008. Sequence-directed DNA export guides chromosome translocation during sporulation in Bacillus subtilis. Nat Struct Mol Biol 15:485–493. [PubMed][CrossRef]
49. Sharp MD, Pogliano K. 1999. An in vivo membrane fusion assay implicates SpoIIIE in the final stages of engulfment during Bacillus subtilis sporulation. ProcNatl Acad Sci USA 96:14553–14558. [PubMed]
50. Fleming TC, Shin JY, Lee SH, Becker E, Huang KC, Bustamante C, Pogliano K. 2010. Dynamic SpoIIIE assembly mediates septal membrane fission during Bacillus subtilis sporulation. Genes Dev 24:1160–1172. [PubMed][CrossRef]
51. Meyer P, Gutierrez J, Pogliano K, Dworkin J. 2010. Cell wall synthesis is necessary for membrane dynamics during sporulation of Bacillus subtilis. Mol Microbiol 76:956–970. [PubMed][CrossRef]
52. Morlot C, Uehara T, Marquis KA, Bernhardt TG, Rudner DZ. 2010. A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis. Genes Dev 24:411–422. [PubMed][CrossRef]
53. Doan T, Coleman J, Marquis KA, Meeske AJ, Burton BM, Karatekin E, Rudner DZ. 2013. FisB mediates membrane fission during sporulation in Bacillus subtilis. Genes Dev 27:322–334. [PubMed][CrossRef]
54. Ramamurthi KS, Losick R. 2009. Negative membrane curvature as a cue for subcellular localization of a bacterial protein. Proc Natl Acad Sci USA 106:13541–13545. [PubMed][CrossRef]
55. Fujita M, Losick R. 2002. An investigation into the compartmentalization of the sporulation transcription factor sigmaE in Bacillus subtilis. Mol Microbiol 43:27–38. [PubMed]
56. Rubio A, Pogliano K. 2004. Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis. EMBO J 23:1636–1646. [PubMed][CrossRef]
57. Diez V, Schujman GE, Gueiros-Filho FJ, de Mendoza D. 2012. Vectorial signalling mechanism required for cell-cell communication during sporulation in Bacillus subtilis. Mol Microbiol 83:261–274. [PubMed][CrossRef]
58. Fawcett P, Melnikov A, Youngman P. 1998. The Bacillus SpoIIGA protein is targeted to sites of spore septum formation in a SpoIIE-independent manner. Mol Microbiol 28:931–943. [PubMed]
59. Chary VK, Xenopoulos P, Eldar A, Piggot PJ. 2010. Loss of compartmentalization of sigma(E) activity need not prevent formation of spores by Bacillus subtilis. J Bacteriol 192:5616–5624. [PubMed][CrossRef]
60. Frandsen N, Stragier P. 1995. Identification and characterization of the Bacillus subtilis spoIIP locus. J Bacteriol 177:716–722. [PubMed]
61. Abanes-De Mello A, Sun YL, Aung S, Pogliano K. 2002. A cytoskeleton-like role for the bacterial cell wall during engulfment of the Bacillus subtilis forespore. Genes Dev 16:3253–3264. [PubMed][CrossRef]
62. Chastanet A, Losick R. 2007. Engulfment during sporulation in Bacillus subtilis is governed by a multi-protein complex containing tandemly acting autolysins. Mol Microbiol 64:139–152. [PubMed][CrossRef]
63. Fredlund J, Broder D, Fleming T, Claussin C, Pogliano K. 2013. The SpoIIQ landmark protein has different requirements for septal localization and immobilization. Mol Microbiol 89:1053–1068. [PubMed][CrossRef]
64. Rodrigues CD, Marquis KA, Meisner J, Rudner DZ. 2013. Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis. Mol Microbiol 89:1039–1052. [PubMed][CrossRef]
65. Aung S, Shum J, Abanes-De Mello A, Broder DH, Fredlund-Gutierrez J, Chiba S, Pogliano K. 2007. Dual localization pathways for the engulfment proteins during Bacillus subtilis sporulation. Mol Microbiol 65:1534–1546. [PubMed][CrossRef]
66. Perez AR, Abanes-De Mello A, Pogliano K. 2000. SpoIIB localizes to active sites of septal biogenesis and spatially regulates septal thinning during engulfment in Bacillus subtilis. J Bacteriol 182:1096–1108. [PubMed]
67. Broder DH, Pogliano K. 2006. Forespore engulfment mediated by a ratchet-like mechanism. Cell 126:917–928. [PubMed][CrossRef]
68. Sun YL, Sharp MD, Pogliano K. 2000. A dispensable role for forespore-specific gene expression in engulfment of the forespore during sporulation of Bacillus subtilis. J Bacteriol 182:2919–2927. [PubMed]
69. Meisner J, Moran CP Jr. 2011. A LytM domain dictates the localization of proteins to the mother cell-forespore interface during bacterial endospore formation. J Bacteriol 193:591–598. [PubMed][CrossRef]
70. Meisner J, Maehigashi T, Andre I, Dunham CM, Moran CP Jr. 2012. Structure of the basal components of a bacterial transporter. Proc Natl Acad Sci USA 109:5446–5451. [PubMed][CrossRef]
71. Levdikov VM, Blagova EV, McFeat A, Fogg MJ, Wilson KS, Wilkinson AJ. 2012. Structure of components of an intercellular channel complex in sporulating Bacillus subtilis. Proc Natl Acad Sci USA 109:5441–5445. [PubMed][CrossRef]
72. Kellner EM, Decatur A, Moran CP Jr. 1996. Two-stage regulation of an anti-sigma factor determines developmental fate during bacterial endospore formation. Mol Microbiol 21:913–924. [PubMed]
73. Camp AH, Losick R. 2008. A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels. Mol Microbiol 69:402–417. [PubMed][CrossRef]
74. Meisner J, Wang X, Serrano M, Henriques AO, Moran CP Jr. 2008. A channel connecting the mother cell and forespore during bacterial endospore formation. Proc Natl Acad Sci USA 105:15100–15105. [PubMed][CrossRef]
75. Camp AH, Losick R. 2009. A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis. Genes Dev 23:1014–1024. [PubMed][CrossRef]
76. Blaylock B, Jiang X, Rubio A, Moran CP Jr, Pogliano K. 2004. Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization. Genes Dev 18:2916–2928. [PubMed][CrossRef]
77. Doan T, Marquis KA, Rudner DZ. 2005. Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum. Mol Microbiol 55:1767–1781. [PubMed][CrossRef]
78. Doan T, Morlot C, Meisner J, Serrano M, Henriques AO, Moran CP Jr, Rudner DZ. 2009. Novel secretion apparatus maintains spore integrity and developmental gene expression in Bacillus subtilis. PLoS Genet 5:e1000566. doi:10.1371/journal.pgen.1000566. [PubMed][CrossRef]
79. Rudner DZ, Pan Q, Losick RM. 2002. Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture. Proc Natl Acad Sci USA 99:8701–8706. [PubMed][CrossRef]
80. Zhang B, Hofmeister A, Kroos L. 1998. The prosequence of pro-sigmaK promotes membrane association and inhibits RNA polymerase core binding. J Bacteriol 180:2434–2441. [PubMed]
81. Resnekov O, Alper S, Losick R. 1996. Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis. Genes Cells 1:529–542. [PubMed]
82. Rudner DZ, Losick R. 2002. A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localization. Genes Dev 16:1007–1018. [PubMed][CrossRef]
83. Campo N, Rudner DZ. 2006. A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis. Mol Cell 23:25–35. [PubMed][CrossRef]
84. Doan T, Rudner DZ. 2007. Perturbations to engulfment trigger a degradative response that prevents cell-cell signalling during sporulation in Bacillus subtilis. Mol Microbiol 64:500–511. [PubMed][CrossRef]
85. Wang KH, Isidro AL, Domingues L, Eskandarian HA, McKenney PT, Drew K, Grabowski P, Chua MH, Barry SN, Guan M, Bonneau R, Henriques AO, Eichenberger P. 2009. The coat morphogenetic protein SpoVID is necessary for spore encasement in Bacillus subtilis. Mol Microbiol 74:634–649. [PubMed][CrossRef]
86. Ramamurthi KS, Losick R. 2008. ATP-driven self-assembly of a morphogenetic protein in Bacillus subtilis. Mol Cell 31:406–414. [PubMed][CrossRef]
87. Price KD, Losick R. 1999. A four-dimensional view of assembly of a morphogenetic protein during sporulation in Bacillus subtilis. J Bacteriol 181:781–790. [PubMed]
88. van Ooij C, Losick R. 2003. Subcellular localization of a small sporulation protein in Bacillus subtilis. J Bacteriol 185:1391–1398. [PubMed]
89. Ramamurthi KS, Clapham KR, Losick R. 2006. Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis. Mol Microbiol 62:1547–1557. [PubMed]
90. Ramamurthi KS, Lecuyer S, Stone HA, Losick R. 2009. Geometric cue for protein localization in a bacterium. Science 323:1354–1357. [PubMed][CrossRef]
91. Ebmeier SE, Tan IS, Clapham KR, Ramamurthi KS. 2012. Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis. Mol Microbiol 84:682–696. [PubMed][CrossRef]
92. McKenney PT, Eichenberger P. 2012. Dynamics of spore coat morphogenesis in Bacillus subtilis. Mol Microbiol 83:245–260. [PubMed][CrossRef]
93. Vasudevan P, Weaver A, Reichert ED, Linnstaedt SD, Popham DL. 2007. Spore cortex formation in Bacillus subtilisis regulated by accumulation of peptidoglycan precursors under the control of sigma K. Mol Microbiol 65:1582–1594. [PubMed][CrossRef]
94. Real G, Fay A, Eldar A, Pinto SM, Henriques AO, Dworkin J. 2008. Determinants for the subcellular localization and function of a nonessential SEDS protein. J Bacteriol 190:363–376. [PubMed][CrossRef]
95. Fay A, Meyer P, Dworkin J. 2010. Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation. J Mol Biol 399:547–561. [PubMed][CrossRef]
96. Fay A, Dworkin J. 2009. Bacillus subtilis homologs of MviN (MurJ), the putative Escherichia coli lipid II flippase, are not essential for growth. J Bacteriol 191:6020–6028. [PubMed][CrossRef]
97. Eichenberger P, Jensen ST, Conlon EM, van Ooij C, Silvaggi J, Gonzalez-Pastor JE, Fujita M, Ben-Yehuda S, Stragier P, Liu JS, Losick R. 2003. The sigmaE regulon and the identification of additional sporulation genes in Bacillus subtilis. J Mol Biol 327:945–972. [PubMed]
98. Popham DL, Stragier P. 1991. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. J Bacteriol 173:7942–7949. [PubMed]
99. Strauss MP, Liew AT, Turnbull L, Whitchurch CB, Monahan LG, Harry EJ. 2012. 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis. PLoS Biol 10:e1001389. doi:10.1371/journal.pbio.1001389. [PubMed][CrossRef]
100. Popham DL, Bernhards CB. Spore peptidoglycan. In Eichenberger P, Driks A (ed), The Bacterial Spore: From Molecules to Systems. ASM Press, Washington, DC, in press.
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2014-02-14
2017-09-25

Abstract:

The Gram-positive bacterium initiates the formation of an endospore in response to conditions of nutrient limitation. The morphological differentiation that spores undergo initiates with the formation of an asymmetric septum near to one pole of the cell, forming a smaller compartment, the forespore, and a larger compartment, the mother cell. This process continues with the complex morphogenesis of the spore as governed by an intricate series of interactions between forespore and mother cell proteins across the inner and outer forespore membranes. Given that these interactions occur at a particular place in the cell, a critical question is how the proteins involved in these processes get properly targeted, and we discuss recent progress in identifying mechanisms responsible for this targeting.

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FIGURE 1

Morphological and protein asymmetry during early stages in sporulation. Following entry into sporulation (i), cells establish an asymmetric septum (ii), dividing the sporangium into two unequally sized compartments, the forespore and the mother cell. During engulfment, the septum begins to curve (iii) and continues to curve (iv) until it is attached to the mother cell by only a small patch. Finally, the forespore pinches off from the mother cell (v) and forms a membrane-bounded compartment containing a thick layer of peptidoglycan (gray). Shown are fluorescent microscopy images using the membrane stain FM4-64 (left) and schematic cartoons (right). FtsZ rings (Z rings; black) are located at mid-cell during growth (left), but upon entry into sporulation (right), are seen initially in a bipolar pattern and eventually in a unipolar pattern before formation of the asymmetric septum. SpoIIE (gray) initially forms “E-rings” that are seen near the bipolar Z rings (left) but following formation of the polar septum (right), SpoIIE is seen on both the mother cell and forespore faces, with apparent enrichment on the forespore face. doi:10.1128/microbiolspec.TBS-0006-2012.f1

Source: microbiolspec February 2014 vol. 2 no. 1 doi:10.1128/microbiolspec.TBS-0006-2012
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FIGURE 2

Localization of septal proteins early in sporulation. The SpoIIIE DNA translocase (red) localizes to the asymmetric septum (i) because of the presence of DNA (blue) and mediates DNA pumping into the forespore (ii). Following completion of septation, SpoIIIE is found in the forespore membrane at the last point of contact with the mother cell (iii). The pro-σ processing enzyme SpoIIGA (yellow) initially localizes to the sites of incipient septum formation (i) and then to the mother cell face of the asymmetric septum (ii). The SpoIIR signaling protein (green) is made in the forespore and crosses the forespore membrane where it presumably interacts with and activates SpoIIGA, although it is also seen in the forespore following completion of septation. SpoIIB (aqua) initially colocalizes with FtsZ (orange) during the process of Z-ring constriction and remains in the polar septum following completion of septation. The SpoIIM (light blue), SpoIIP (dark blue), and SpoIID (purple) proteins proceed to localize to the now curved asymmetric septum. doi:10.1128/microbiolspec.TBS-0006-2012.f2

Source: microbiolspec February 2014 vol. 2 no. 1 doi:10.1128/microbiolspec.TBS-0006-2012
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FIGURE 3

Localization of septal proteins later in sporulation. Expression of SpoIIIAH (lime) is under control of σ and it is initially found in all of the mother cell membrane (i). Expression of SpoIIQ (purple) is under control of σ and it is initially found in the forespore septal membrane. Interaction of SpoIIQ and SpoIIIAH in the septal intermembrane space leads to localization of SpoIIIAH to the septum (ii), and this interaction continues until late in engulfment (iii). Initially, contact between SpoIIQ in the forespore membrane and SpoIIIAH in the mother cell membrane is prevented because of the presence of peptidoglycan. However, removal of this layer allows contact between the two proteins presumably through “extracellular” domains, resulting in the enrichment of SpoIIIAH at the septum. SpoIVFB (red) is initially observed in all mother cell membranes, but it eventually is “captured” by SpoIVFA (orange) and becomes enriched at the forespore in a complex with the SpoIVFB and BofA. SpoIVFA interacts with a number of proteins in the forespore outer membrane including SpoIID (green), SpoIIP (dark blue), SpoIIM (light blue), SpoIIIAH (lime), and SpoIIQ (purple). doi:10.1128/microbiolspec.TBS-0006-2012.f3

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FIGURE 4

Localization of proteins involved in spore coat and cortex assembly. SpoVM (green) has an intrinsic affinity for the forespore. SpoVD (red) and SpoVE (orange) form a complex at the outer forespore membrane. In the absence of SpoVE, SpoVD is found throughout the mother cell membrane. doi:10.1128/microbiolspec.TBS-0006-2012.F4

Source: microbiolspec February 2014 vol. 2 no. 1 doi:10.1128/microbiolspec.TBS-0006-2012
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