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Chapter 14 : Conjugation in Gram-Positive Bacteria

Authors: Nikolaus Goessweiner-Mohr1, Karsten Arends2, Walter Keller3, Elisabeth Grohmann4
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Affiliations: 1: Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria; 2: Robert Koch-Institute, Nordufer 20, 13353 Berlin, Germany; 3: Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria; 4: Faculty of Biology, Microbiology, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany; 5: Division of Infectious Diseases, University Medical Centre Freiburg, 79106 Freiburg, Germany
Content Type: Monograph
Publication Year: 2015

Category: Clinical Microbiology

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Abstract:

Conjugative transfer is an important driver in evolution, enabling bacteria to acquire new traits ( ). During conjugative transfer, DNA translocation across the cell envelopes of two cells forming a mating pair is mediated by two types of mobile genetic elements: conjugative plasmids and integrating conjugative elements (ICEs) ( ). Most conjugative plasmids apply a sophisticated multiprotein secretion apparatus, the so-called type IV secretion system (T4SS) to transfer DNA to a recipient cell ( ). Conjugative T4SSs of Gram-positive (G+) bacteria exhibit considerable similarities to their Gram-negative (G–) counterparts; the first steps processing the plasmid DNA to be transferred with the relaxase, covalently attached to its 5′ end, are virtually identical ( ). However, the actual DNA translocation process including the passage of the cell envelope of the donor and the recipient cell appears to differ considerably between G+ and G– bacteria. This might be due to the differences in the structure of the cell envelope: cytoplasmic membrane followed by a thick multilayered peptidoglycan (PG) in G+ bacteria versus a two-membrane configuration with periplasmic space and thin PG layer between the two membranes in G– bacteria. Therefore, it is not surprising that homologs of VirB7, VirB9, and VirB10 proteins identified as actual G– T4SS channel components ( ) have not been detected so far in G+ T4SSs.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Conjugation in Gram-Positive Bacteria
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Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
/content/10.1128/9781555818982.chap14.fig14-1
Figure 1
Genetic organization of the pIP501 operon. Proteins with sequence similarities with the corresponding Ti-plasmid VirB/D4, pCF10, and pCW3 T4SS proteins are in blue; the potential two-protein-coupling protein (consisting of TraI and TraJ) is indicated with brackets; relations based on structure (TraM C-terminal domain, VirB8-like [ ]) and domain prediction (TraL, VirB6-like) based similarities are in yellow; the gene encoding the putative relaxase is in green. The respective protein families are indicated. P, operon promoter. The genes of the pIP501 region are drawn to scale. Put., putative.
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Figure 1

Genetic organization of the pIP501 operon. Proteins with sequence similarities with the corresponding Ti-plasmid VirB/D4, pCF10, and pCW3 T4SS proteins are in blue; the potential two-protein-coupling protein (consisting of TraI and TraJ) is indicated with brackets; relations based on structure (TraM C-terminal domain, VirB8-like [ ]) and domain prediction (TraL, VirB6-like) based similarities are in yellow; the gene encoding the putative relaxase is in green. The respective protein families are indicated. P, operon promoter. The genes of the pIP501 region are drawn to scale. Put., putative.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 2
Model of the pIP501 DNA transfer pathway. First, is bound by the relaxase TraA. After being nicked, the single-stranded plasmid is recruited to the putative transfer channel (modified from reference 17) via the putative two-protein coupling protein TraJ. Decreased shading of PG symbolizes TraG-mediated local opening of PG. The localization and orientation of the T4SS proteins is based on predictions and localization studies ( ). The N terminus of the T4SS proteins is marked (N). Arrows indicate protein-protein interactions determined by yeast-two-hybrid studies and validated by pull-down assays ( ), as well as interactions found by using the Thermofluor method (Goessweiner-Mohr et al., unpublished data). The thickness of the arrows marks the strength of the detected interactions. The putative function of key members of the pIP501 operon in the DNA secretion process is indicated. PG, peptidoglycan; CM, cytoplasmic membrane; CP, cytoplasm.
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Figure 2

Model of the pIP501 DNA transfer pathway. First, is bound by the relaxase TraA. After being nicked, the single-stranded plasmid is recruited to the putative transfer channel (modified from reference 17) via the putative two-protein coupling protein TraJ. Decreased shading of PG symbolizes TraG-mediated local opening of PG. The localization and orientation of the T4SS proteins is based on predictions and localization studies ( ). The N terminus of the T4SS proteins is marked (N). Arrows indicate protein-protein interactions determined by yeast-two-hybrid studies and validated by pull-down assays ( ), as well as interactions found by using the Thermofluor method (Goessweiner-Mohr et al., unpublished data). The thickness of the arrows marks the strength of the detected interactions. The putative function of key members of the pIP501 operon in the DNA secretion process is indicated. PG, peptidoglycan; CM, cytoplasmic membrane; CP, cytoplasm.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 3
Comparison of the domain arrangement and classification of putative lytic transglycosylases from G+ and G– putative T4SSs. TraG (pIP501), TcpG (pCW3), VirB1 (Ti-plasmid), and PrgK (pCF10) were chosen as representatives of their respective classes. The potential SLT and CHAP(-like) domains were assigned according to secondary structure predictions with PSIPred ( ). TMHs were annotated with HMMTOP ( ).
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Figure 3

Comparison of the domain arrangement and classification of putative lytic transglycosylases from G+ and G– putative T4SSs. TraG (pIP501), TcpG (pCW3), VirB1 (Ti-plasmid), and PrgK (pCF10) were chosen as representatives of their respective classes. The potential SLT and CHAP(-like) domains were assigned according to secondary structure predictions with PSIPred ( ). TMHs were annotated with HMMTOP ( ).

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 4a
Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.
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Image of Figure 4a
Figure 4a

Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 4b
Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.
10.1128/9781555818982/fig14-4b_thmb.gif
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Image of Figure 4b
Figure 4b

Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 4c
Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.
10.1128/9781555818982/fig14-4c_thmb.gif
10.1128/9781555818982/fig14-4c.gif
Image of Figure 4c
Figure 4c

Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 4d
Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.
10.1128/9781555818982/fig14-4d_thmb.gif
10.1128/9781555818982/fig14-4d.gif
Image of Figure 4d
Figure 4d

Secondary structure-based classification of lytic transglycosylases. A, class α, B, class β, C, class γ, D, class δ lytic transglycosylases. Secondary structure (PSIpred) and TM motif (HMMTOP) prediction for G– and G+ lytic transglycosylases from conjugative plasmids, transposons, ICEs, and GIs; alpha helices (blue), beta strands (red), and TM motifs (boxes) are highlighted; the putative N-terminal ends of the SLT and CHAP(-like) domains are indicated.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Figure 5
Comparison of the domain arrangement and classification of VirB6-like proteins from G+ and G– putative T4SSs. TraL (pIP501), PrgH (pCF10), TcpH (pCW3), VirB6 (Ti-plasmid), TraD (pKM101), TraG (R1 plasmid), and TrbP (pBP136) were selected as representatives of their respective classes. Predicted TMHs (HMMTOP [ ]) are represented as gray boxes.
10.1128/9781555818982/fig14-5_thmb.gif
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Image of Figure 5
Figure 5

Comparison of the domain arrangement and classification of VirB6-like proteins from G+ and G– putative T4SSs. TraL (pIP501), PrgH (pCF10), TcpH (pCW3), VirB6 (Ti-plasmid), TraD (pKM101), TraG (R1 plasmid), and TrbP (pBP136) were selected as representatives of their respective classes. Predicted TMHs (HMMTOP [ ]) are represented as gray boxes.

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
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Tables

Conjugation in Gram-Positive Bacteria
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Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013
/content/10.1128/9781555818982.chap14.tab14-1
Table 1
Classification of TraG-like and other lytic transglycosylases
Generic image for table
Table 1

Classification of TraG-like and other lytic transglycosylases

Citation: Goessweiner-Mohr N, Arends K, Keller W, Grohmann E. 2015. Conjugation in Gram-Positive Bacteria, p 237-256. In Tolmasky M, Alonso J (ed), Plasmids: Biology and Impact in Biotechnology and Discovery. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PLAS-0004-2013

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