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Review

Bacterial Growth and Cell Division: a Mycobacterial Perspective

Erik C. Hett, Eric J. Rubin
Erik C. Hett
Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115
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Eric J. Rubin
Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115
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  • For correspondence: erubin@hsph.harvard.edu
DOI: 10.1128/MMBR.00028-07
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  • FIG. 1.
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    FIG. 1.

    Diagram of the basic components of the mycobacterial cell wall. MAPc, MA-AG-PG complex.

  • FIG. 2.
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    FIG. 2.

    Synthesis of PG. Major steps are shown, with precursors such as UDP-NAM, lipid I, and lipid II being synthesized within the cytoplasm. Lipid II is then transported across the lipid membrane, and periplasmic transglycosylases and endopeptidases link the PG monomer into existing PG sheets through β-1,4 glycosidic linkages and DAP-DAP peptide cross-linkages.

  • FIG. 3.
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    FIG. 3.

    Localization of nascent and inert PG in different bacteria.

  • FIG. 4.
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    FIG. 4.

    V-snapping process of mycobacteria during cell division.

  • FIG. 5.
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    FIG. 5.

    Cycle of mycobacteria entering and exiting dormancy. Environmental conditions and proteins thought to be involved with inducing transitions between the two life cycle stages are listed.

Tables

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  • TABLE 1.

    Attributes of mycobacterial PG and their biological significance

    Mycobacterial PG attributeCommon PG attribute in other bacteriaBiological significance
    DAP-DAP and DAP-Ala peptide cross-linkageDAP-Ala peptide cross-linkageMay provide increased rigidity to the PG to help survive stressful conditions
    N-Glycoylmuramic acid and NAMNAMCould tighten the PG sacculus by providing more opportunities for hydrogen bonding and increase resistance to β-lactams and lysozyme
    Amidated l-Glu and DAPAmidated l-Glu and DAPMay play a role in the regulation of cross-linking and could increase resistance to hydrolysis by specific endopeptidases, as seen with the amidation of PG sugar residues increasing resistance to muramidase
    d-Glutamate or l-alanine modified with glycineNo modificationUnknown
  • TABLE 2.

    Bacterial cytoskeletal elements

    Cytoskeletal elementProteinFunctionM. tuberculosis homologue(s)
    TubulinFtsZForms a structural ring that recruits proteins necessary for the synthesis of septal PGFtsZ (Rv2150c)
    ActinMreB (Mbl, MreBH)Cell shape, guides PG synthesisNone
    ParMDNA partitioningParA (Rv3918c), ParB (Rv3917c)
    MamKOrganelle positioning?
    Intermediate filamentCreSDetermines the specialized crescent shapeNone
  • TABLE 3.

    Divisome proteins encoded in different bacterial genomes

    DivisomeaFunctionHomologueb in:
    E. coliB. subtilisS. coelicolorM. tuberculosis
    FtsAPositive regulator of FtsZ assembly, membrane associated, actin like++−−
    FtsBBridge cytoplasmic with periplasmic, transmembrane, forms tripartite complex with FtsL and FtsQ+DivICDivIC?
    FtsEUnknown, ABC transporter family++−+
    FtsISynthesize septal PG, transpeptidase (PBP 3)++++
    FtsKDNA partitioning, large multifunctional membrane protein+SpoIIIE++
    FtsLBridge cytoplasmic with periplasmic, transmembrane, forms tripartite complex with FtsB and FtsQ+++−
    FtsNUnknown, weak homology to amidase, binds PG+−−−
    FtsQBridge cytoplasmic with periplasmic, many protein-protein interactions, transmembrane+DivIB++
    FtsWPredicted transporter of PG precursors, multitransmembrane protein+++Interacts with FtsZ and FtsI and may substitute for lack of ZipA or FtsA
    FtsXUnknown, ABC transporter family+?−+
    FtsZInitiates Z ring, helps constrict ring, tubulin like, GTPase++++
    ZipAPositive regulator of FtsZ assembly, membrane associated+ZapA−−
    AmiCSeparates daughter cells by hydrolyzing septal PG, amidase+???
    EnvCSeparates daughter cells by hydrolyzing septal PG, hydrolase+???
    • ↵ a FtsH, FtsJ, and FtsY are not involved in cell division (FtsY has pleitropic effects on cell division).

    • ↵ b +, present in genome; −, not found in genome; ?, other homologues may exist.

  • TABLE 4.

    Inhibitors of FtsZ assembly

    InhibitorFunctionHomologuea in:
    E. coliB. subtilisS. coelicolorM. tuberculosis
    EzrANegative regulator of FtsZ assembly, topology similar to that of ZapA?+?−
    MinCNegative regulator of FtsZ assembly at poles, binds and oscillates between poles with MinD++−−
    MinDOscillates MinC from pole to pole, ATPase, binds to membrane until MinE stimulates ATP hydrolysis++−−
    MinESweeps MinCD complex from one pole to the other, stimulates MinD ATPase and release of MinCD from membrane+DivIVA; rather than oscillating between poles, remains at poles, tethering MinCD complexDivIVADivIVA orthologue, Ag84, encoded by wag31
    SulANegative regulator of FtsZ assembly, induced by SOS response+YneA, structurally unrelated to SulA but functionally similar?−
    SepFUnknown, interacts with FtsZ and localization depends on FtsZ?+??
    SlmANegative regulator of FtsZ assembly, prevents septum assembly over nucleoid (nucleoid occlusion)+−??
    NocNegative regulator of FtsZ assembly, prevents septum assembly over nucleoid (nucleoid occlusion)?+??
    CrgANegative regulator of FtsZ assembly−−++ (Rv0011c)
    • ↵ a +, present in genome; −, not found in genome; ?, other homologues may exist.

  • TABLE 5.

    Mycobacterial growth regulatory systems

    Growth regulatory system(s)MechanismMycobacterial protein(s)Function
    STPKsSensors of environmental signals that regulate host-pathogen interactions and developmental changes through signal transduction using reversible phosphorylation of proteins; M. tuberculosis encodes 12 STPKsPknARegulates cell shape; essential; transmembrane
    PknBRegulates cell shape; essential; transmembrane
    PknFPhosphorylates putative ABC transporter of M. tuberculosis (Rv1747); transmembrane
    PknGModulates macrophage response to infection; essential; soluble
    PknHPhosphorylates the OmpR-like EmbR transcription factor; transmembrane
    PknKSoluble
    PknC, -D, -E, -I, -J, -LTransmembrane
    WhiB genesThought to bind DNA and influence transcription as well as play a role in sensing intracellular redox state; M. tuberculosis encodes 7 WhiB homologuesWhiB2Possibly involved in cell wall remodeling and cell division
    WhiB3Interacts with RpoV and is important for pathogenesis within the host
    WhiB4May be a sensor of oxidative stress
    WhiB1, -5, -6, -7Unknown
    TCSsTransfers a phosphate from the histidine residue on the autophosphorylated sensor to the aspartate residue on the response regulator to relay signals from the environment; M. tuberculosis encodes 11 TCSs in total (some not listed)DosRS/TDormancy survival
    MtrABProliferation in macrophages
    SenX3-RegX3May regulate phosphate-dependent gene expression
    MprABGrowth during persistent stage
    PhoPRImplicated in regulating production of complex cell wall lipids
    Alternative sigma factorsThe largest subset are known as ECF sigma factors and are small regulatory proteins lacking some of the conserved regions of typical sigma factors; M. tuberculosis encodes 13 sigma factors, 10 of which are ECF sigma factors (some not listed)SigB, -D, -E, -HRegulate genes that allow bacteria to adapt to stress
    TA systemOriginally recognized as a mechanism for ensuring proper plasmid segregation, the TA loci have now been shown to have diverse roles; works by production of a stable toxin and an unstable antitoxin, thus requiring a constant supply of antitoxin; M. tuberculosis has 38 TA loci (some not listed)3 RelBE homologues and 9 MazEF homologuesToxins that cleave mRNA in response to nutrient stress or starvation
    Stringent responseRelA is triggered by uncharged tRNAs at the ribosomal A site during carbon starvation and synthesizes P4G, which binds RNA polymerase, reducing the promoter open-complex half-life and halting translationRelASynthesizes P4G
    SpoTHydrolyzes P4G
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Bacterial Growth and Cell Division: a Mycobacterial Perspective
Erik C. Hett, Eric J. Rubin
Microbiology and Molecular Biology Reviews Mar 2008, 72 (1) 126-156; DOI: 10.1128/MMBR.00028-07

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Bacterial Growth and Cell Division: a Mycobacterial Perspective
Erik C. Hett, Eric J. Rubin
Microbiology and Molecular Biology Reviews Mar 2008, 72 (1) 126-156; DOI: 10.1128/MMBR.00028-07
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  • Top
  • Article
    • SUMMARY
    • INTRODUCTION
    • CELL WALL COMPONENTS
    • MAINTENANCE OF SHAPE
    • BACTERIAL CELL DIVISION
    • REGULATION OF BACTERIAL GROWTH AND DIVISION
    • CELL DIVISION UNDER SPECIALIZED CONDITIONS
    • CONCLUSIONS
    • ACKNOWLEDGMENTS
    • REFERENCES
  • Figures & Data
  • Info & Metrics
  • PDF

KEYWORDS

Cell Division
Mycobacterium

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