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12 The MmpL Protein Family

Authors: Madhulika Jain1, Eric D. Chow2, Jeffery S. Cox3
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Affiliations: 1: Department of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143-2200; 2: Department of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143-2200; 3: Department of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143-2200
Content Type: Monograph
Publication Year: 2008
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Abstract:

The diverse array of lipids, many of which are critical for virulence and mediate interactions with host cells, exist primarily on the outermost surface of the bacterium. Fourteen genes have been identified by analysis of the two completed genomic sequences. These genes encode for large, multitransmembrane containing proteins and were thus given the moniker MmpL (for mycobacterial membrane protein, large). Initial models of MmpL function were based on the RND transporters from gram-negative bacteria. MmpL7 was the first MmpL family member to be studied and was identified as required for virulence and bacterial growth in vivo in a mouse model of infection. Mutants in were also isolated in a signature- tagged mutagenesis screen, and MmpL8 is indispensable for growth and virulence in mice. First, transcription is induced, albeit modestly, during infection of activated macrophages. The eukaryotic larger resistance, nodulation, and division (RND-family member, Niemann-Pick C1 (NPC1) utilizes the proton motive force to translocate cholesterol across the cell membrane and it is widely thought that RND family members use proton antiport or symport as a mechanism of facilitated transport of their substrates. The Lol system functions to export lipoproteins across the periplasm of to the inner leaflet of the outer membrane. LolCDE bind specifically to lipoproteins destined for the outer membrane and export them across the cell membrane, where they bind the periplasmic shuttle LolA.

Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12

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Integral Membrane Proteins
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Outer Membrane Proteins
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12 The MmpL Protein Family
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Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12
/content/10.1128/9781555815783.ch12.ch12fig01
Figure 1.
Phylogenetic tree of MmpL proteins from sequenced mycobacterial species. The MmpLs from are shown in bold. Most of the orthologues of the MmpLs are omitted because they are identical in sequence except Mb1177, which has a frameshift mutation in , and Mb1583, which is a full-length version of MmpL6. Mb, ; ML, ; MAP, ; MM, ; MUL, ; MSMEG, .
10.1128/9781555815783/f0202-01_thmb.gif
10.1128/9781555815783/f0202-01.gif
Image of Figure 1.
Figure 1.

Phylogenetic tree of MmpL proteins from sequenced mycobacterial species. The MmpLs from are shown in bold. Most of the orthologues of the MmpLs are omitted because they are identical in sequence except Mb1177, which has a frameshift mutation in , and Mb1583, which is a full-length version of MmpL6. Mb, ; ML, ; MAP, ; MM, ; MUL, ; MSMEG, .

Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12
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Figure 2.
Predicted membrane topology of MmpLs, indicating the two non-transmembrane regions.
10.1128/9781555815783/f0203-01_thmb.gif
10.1128/9781555815783/f0203-01.gif
Image of Figure 2.
Figure 2.

Predicted membrane topology of MmpLs, indicating the two non-transmembrane regions.

Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12
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Figure 3.
Gene organization of MmpLs. Genes predicted to be involved in lipid transport, including the and genes, the and genes, and the operon are shown as white arrows. Genes predicted to be involved in lipid biosynthesis and metabolism are shown in black.
10.1128/9781555815783/f0204-01_thmb.gif
10.1128/9781555815783/f0204-01.gif
Image of Figure 3.
Figure 3.

Gene organization of MmpLs. Genes predicted to be involved in lipid transport, including the and genes, the and genes, and the operon are shown as white arrows. Genes predicted to be involved in lipid biosynthesis and metabolism are shown in black.

Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12
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Figure 4.
Model of MmpL secretion. The proposed models for PDIM and SL-1 secretion through MmpL7 and MmpL8, respectively, are shown. PpsA-E and Mas are polyketide synthases that extend straight chain fatty acids to phthiocerol and mycocerosic acid, respectively ( ). The enzymes FadD26 and FadD28 are thought to be AMP ligases that activate straight-chain fatty acids for transfer to the Pps and Mas enzymes ( ). The thioesterase TesA is also required for the synthesis of PDIM and interacts with PpsE ( ). PapA5 is able to catalyze the esterification of mycocerosic acids to phthiocerol to form PDIM ( ). MmpL7 and DrrABC are required to transport PDIM across the cell membrane ( ). Finally, LppX is a signal sequence containing protein that is thought to transport PDIM across the periplasm to the cell wall ( ). Two models for SL-1 secretion are shown. Pks2 is required for the synthesis of SL ( ). In model A, MmpL8 recruits an as yet unidentified biosynthetic factor to complete the synthesis of SL-1 from SL, before transport across the cell membrane ( ). In model B, MmpL8 exports SL across the cell membrane, after which it is converted to SL-1 by an as yet unidentified enzyme ( ). CM, cytoplasmic membrane; PG, peptidoglycan; mAG, mycolyl-arabinogalactan.
10.1128/9781555815783/f0207-01_thmb.gif
10.1128/9781555815783/f0207-01.gif
Image of Figure 4.
Figure 4.

Model of MmpL secretion. The proposed models for PDIM and SL-1 secretion through MmpL7 and MmpL8, respectively, are shown. PpsA-E and Mas are polyketide synthases that extend straight chain fatty acids to phthiocerol and mycocerosic acid, respectively ( ). The enzymes FadD26 and FadD28 are thought to be AMP ligases that activate straight-chain fatty acids for transfer to the Pps and Mas enzymes ( ). The thioesterase TesA is also required for the synthesis of PDIM and interacts with PpsE ( ). PapA5 is able to catalyze the esterification of mycocerosic acids to phthiocerol to form PDIM ( ). MmpL7 and DrrABC are required to transport PDIM across the cell membrane ( ). Finally, LppX is a signal sequence containing protein that is thought to transport PDIM across the periplasm to the cell wall ( ). Two models for SL-1 secretion are shown. Pks2 is required for the synthesis of SL ( ). In model A, MmpL8 recruits an as yet unidentified biosynthetic factor to complete the synthesis of SL-1 from SL, before transport across the cell membrane ( ). In model B, MmpL8 exports SL across the cell membrane, after which it is converted to SL-1 by an as yet unidentified enzyme ( ). CM, cytoplasmic membrane; PG, peptidoglycan; mAG, mycolyl-arabinogalactan.

Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12
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Tables

12 The MmpL Protein Family
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Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12
/content/10.1128/9781555815783.ch12.ch12tab01
Table 1.
Distribution of MmpL transporters in mycobacteria
Generic image for table
Table 1.

Distribution of MmpL transporters in mycobacteria

Citation: Jain M, Chow E, Cox J. 2008. 12 The MmpL Protein Family, p 201-209. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch12

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