Present address: Laboratory of Molecular Bacteriology, Department of Medical Microbiology, University Medical Center Groningen, Hanzeplein 1, 9700 RB, Groningen, the Netherlands;
LysM, a widely distributed protein motif for binding to (peptido)glycans
Article first published online: 8 APR 2008
© 2008 The Authors; Journal compilation © 2008 Blackwell Publishing Ltd
Volume 68, Issue 4, pages 838–847, May 2008
How to Cite
Buist, G., Steen, A., Kok, J. and Kuipers, O. P. (2008), LysM, a widely distributed protein motif for binding to (peptido)glycans. Molecular Microbiology, 68: 838–847. doi: 10.1111/j.1365-2958.2008.06211.x
- Issue published online: 8 APR 2008
- Article first published online: 8 APR 2008
- Accepted 8 March, 2008.
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner to peptidoglycan, using specific protein domains, such as the prominent LysM (Lysin Motif) domain. More than 4000 (Pfam PF01476) proteins of both prokaryotes and eukaryotes have been found to contain one or more Lysin Motifs. Notably, this collection contains not only truly secreted proteins, but also (outer-)membrane proteins, lipoproteins or proteins bound to the cell wall in a (non-)covalent manner. The motif typically ranges in length from 44 to 65 amino acid residues and binds to various types of peptidoglycan and chitin, most likely recognizing the N-acetylglucosamine moiety. Most bacterial LysM-containing proteins are peptidoglycan hydrolases with various cleavage specificities. Binding of certain LysM proteins to cells of Gram-positive bacteria has been shown to occur at specific sites, as binding elsewhere is hindered by the presence of other cell wall components such as lipoteichoic acids. Interestingly, LysM domains of certain plant kinases enable the plant to recognize its symbiotic bacteria or sense and induce resistance against fungi. This interaction is triggered by chitin-like compounds that are secreted by the symbiotic bacteria or released from fungi, demonstrating an important sensing function of LysMs.