<b>The S‐layer protein of <i>Corynebacterium glutamicum</i> is anchored to the cell wall by its C‐terminal hydrophobic domain</b>

Chami, Mohamed; Bayan, Nicolas; Peyret, Jean Louis; Gulik-Krzywicki, T.; Leblon, Gérard; Shechter, Emanuel

doi:10.1046/j.1365-2958.1997.d01-1868.x

Cited by 65 publications

(52 citation statements)

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“…PS2 is an S-layer protein that forms a 2D crystal network at the cell surface (16,44). Its C-terminal hydrophobic domain has been described to be essential to its association with the cell envelope (17). The presence of PS2 in ⌬aftB OMFs is in good agreement with all previous published data and suggests that the C-terminal stretch of hydrophobic amino acids provides a physical anchor into the mycolate outer membrane.…”

Section: Discussionsupporting

confidence: 80%

“…This protein, encoded by cspB, forms a crystalline surface layer (S layer) covering the whole surface of strain CGL 2005 and several other C. glutamicum strains (but not ATCC 13032) (27,44). Its C-terminal hydrophobic sequence was shown to be essential for cell wall anchoring (17) and thus was proposed to be the insert in the outer membrane. The similarity of the C-terminal domains between NCgl0381 and PS2 suggests that both proteins are physically associated to the outer membrane of C. glutamicum.…”

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A Deficiency in Arabinogalactan Biosynthesis AffectsCorynebacterium glutamicumMycolate Outer Membrane Stability

et al. 2010

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Corynebacterineae is a specific suborder of Gram-positive bacteria that includes Mycobacterium tuberculosis and Corynebacterium glutamicum. The ultrastructure of the cell envelope is very atypical. It is composed of a heteropolymer of peptidoglycan and arabinogalactan (AG) covalently associated to an outer membrane. Five arabinosyltransferases are involved in the biosynthesis of AG in C. glutamicum. AftB catalyzes the transfer of Araf (arabinofuranosyl) onto the arabinan domain of the arabinogalactan to form terminal ␤(1 3 2)-linked Araf residues. Here we show that ⌬aftB cells lack half of the arabinogalactan mycoloylation sites but are still able to assemble an outer membrane. In addition, we show that a ⌬aftB mutant grown on a rich medium has a perturbed cell envelope and sheds a significant amount of membrane fragments in the external culture medium. These fragments contain mono-and dimycolate of trehalose and PorA/H, the major porin of C. glutamicum, but lack conventional phospholipids that typify the plasma membrane, suggesting that they are derived from the atypical mycolate outer membrane of the cell envelope. This is the first report of outer membrane destabilization in the Corynebacterineae, and it suggests that a strong interaction between the mycolate outer membrane and the underlying polymer is essential for cell envelope integrity. The presence of outer membrane-derived fragments (OMFs) in the external medium of the ⌬aftB mutant is also a very promising tool for outer membrane characterization. Indeed, fingerprint analysis of major OMF-associated proteins has already led to the identification of 3 associated mycoloyltransferases and an unknown protein with a C-terminal hydrophobic anchoring domain reminiscent of that found for the S-layer protein PS2 of C. glutamicum.Corynebacterineae is a specific suborder of Gram-positive bacteria that includes medically and economically important species, such as Mycobacterium tuberculosis, Mycobacterium leprae, and Corynebacterium glutamicum. The ultrastructure of cell envelopes in the Corynebacterineae has been intensively studied during recent decades and has revealed a completely unexpected scheme. Indeed, they are composed of a heteropolymer of peptidoglycan and arabinogalactan (AG) covalently associated to an outer membrane. This outer membrane is made up of mycolic acids that either esterify trehalose (free mycolates) or are terminal Araf residues of AG skeleton (bound mycolates) (38-40). The disclosure of this very atypical structure initially came from functional studies in which pore-forming proteins were identified in almost all members of the Corynebacterineae (41, 62), pointing out the presence of an unexpected additional hydrophobic barrier in the cell envelope of these Gram-positive bacteria.

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A Deficiency in Arabinogalactan Biosynthesis AffectsCorynebacterium glutamicumMycolate Outer Membrane Stability

et al. 2010

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“…The S-layer protein of C. glutamicum ATCC 17965 has a hydrophobic C-terminal end which binds to a hydrophobic cell wall layer possessing a high content of mycolic acids (21). In archaea missing a rigid cell wall layer, the S-layer subunits closely interact with the plasma membrane.…”

Section: Attachment Of S-layer Proteins To the Underlying Cell Envelomentioning

confidence: 99%

S-Layer Proteins

2000

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“…The PS2 protein of C. glutamicum ATCC 17965 exhibits no similarities to any other protein in the EMBL database (Peyret et al, 1993). The hydrophobic C-terminus of the PS2 protein was found to be involved in the attachment of PS2 to the cell wall (Chami et al, 1997). The S-layer of C. glutamicum ATCC 17965 is characterized by a hexagonal lattice symmetry (Chami et al, 1995).…”

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confidence: 99%

Classification of hyper-variable Corynebacterium glutamicum surface-layer proteins by sequence analyses and atomic force microscopy

Hansmeier

Bartels

Ros

et al. 2004

Journal of Biotechnology

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The structural S-layer proteins of 28 different Corynebacterium glutamicum isolates have been analyzed systematically. Treatment of whole C. glutamicum cells with detergents resulted in the isolation of S-layer proteins with different apparent molecular masses, ranging in size from 55 to 66 kDa. The S-layer genes analyzed were characterized by coding regions ranging from 1473 to 1533 nucleotides coding for S-layer proteins with a size of 490-510 amino acids. Using PCR techniques, the corresponding S-layer genes of the 28 C. glutamicum isolates were all cloned and sequenced. The deduced amino acid sequences of the S-layer proteins showed identities between 69 and 98% and could be grouped into five phylogenetic classes. Furthermore, sequence analyses indicated that the S-layer proteins of the analyzed C. glutamicum isolates exhibit a mosaic structure of highly conserved and highly variable regions. Several conserved regions were assumed to play a key role in the formation of the C. glutamicum S-layers. Especially the N-terminal signal peptides and the C-terminal anchor sequences of the S-layer proteins showed a nearly perfect amino acid sequence conservation. Analyses by atomic force microscopy revealed a committed hexagonal structure. Morphological diversity of the C. glutamicum S-layers was observed in a class-specific unit cell dimension (ranging from 15.2 to 17.4 nm), which correlates with the sequence similarity-based classification. It could be demonstrated that differences in the primary structure of the S-layer proteins were reflected by the S-layer morphology.

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**The S‐layer protein of Corynebacterium glutamicum is anchored to the cell wall by its C‐terminal hydrophobic domain**

Cited by 65 publications

References 39 publications

A Deficiency in Arabinogalactan Biosynthesis AffectsCorynebacterium glutamicumMycolate Outer Membrane Stability

A Deficiency in Arabinogalactan Biosynthesis AffectsCorynebacterium glutamicumMycolate Outer Membrane Stability

S-Layer Proteins

Classification of hyper-variable Corynebacterium glutamicum surface-layer proteins by sequence analyses and atomic force microscopy

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