Expression of C-terminal Repeat Region of Peptidoglycan Hydrolase of Lactococcus lactis IL1403 in Methylotrophic Yeast Pichia pastoris

Tarahomjoo, Shirin; Katakura, Yoshio; Shioya, Suteaki

doi:10.1263/jbb.105.134

Cited by 13 publications

(14 citation statements)

References 28 publications

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“…Binding improved considerably when the entire LysM Mbg domain, with both motifs, was coupled two or three times to the N-terminus of GFP. Of a C-terminal fusion of LysM AcmA with S. bovis α-amylase, only 9 % ended up in the soluble fraction of the producer in E. coli (Tarahomjoo et al 2008a, b). Upon expressing the LysM AcmA domain on its own in this host, 20 % of it ended up in the soluble fraction.…”

Section: Display Of Proteins Peptides and Enzymesmentioning

confidence: 99%

Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications

Visweswaran

Leenhouts²,

Roosmalen³

et al. 2014

Appl Microbiol Biotechnol

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The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has been shown to bind noncovalently to peptidoglycan and chitin by interacting with N-acetylglucosamine moieties. The LysM sequence is present singly or repeatedly in a large number of proteins of prokaryotes and eukaryotes. Since the mid-1990s, domains containing one or more of these LysM sequences originating from different LysM-containing proteins have been examined for purely scientific reasons as well as for their possible use in various medical and industrial applications. These studies range from detecting localized binding of LysM-containing proteins onto bacteria to actual bacterial cell surface analysis. On a more applied level, the possibilities of employing the LysM domains for cell immobilization, for the display of peptides, proteins, or enzymes on (bacterial) surfaces as well as their utility in the development of novel vaccines have been scrutinized. To serve these purposes, the chimeric proteins containing one or more of the LysM sequences have been produced and isolated from various prokaryotic and eukaryotic expression hosts. This review gives a succinct overview of the characteristics of the LysM domain and of current developments in its application potential.

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Section: Display Of Proteins Peptides and Enzymesmentioning

confidence: 99%

Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications

Visweswaran

Leenhouts²,

Roosmalen³

et al. 2014

Appl Microbiol Biotechnol

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“…However, its dissociation rate constant from the cell surface was 3.5 fold lower than that of CphI. These results indicated that the protein engineering approaches can be useful for increasing the binding stability of noncovalent anchors (Tarahomjoo et al 2008b). …”

Section: Development Of Whole Cell Biocatalystsmentioning

confidence: 92%

Exploring Surface Display Technology for Enhancement of Delivering Viable Lactic Acid Bacteria to Gastrointestinal Tract

Tarahomjoo¹

2013

Lactic Acid Bacteria - R &Amp; D for Food, Health and Livestock Purposes

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“…More than 4,000 proteins in prokaryotes and eukaryotes contain the highly conserved LysM domain (Buist et al 2008), which allows these proteins to bind to the peptidoglycan layer of bacterial cell walls in a non-covalent manner (Steen et al 2003; Tarahomjoo et al 2008). LysM was first discovered as a C-terminal motif in the lysozyme of Bacillus subtilis phage ø29.…”

Section: Lysm and Pmb Domain-containing Cell Wall Hydrolasesmentioning

confidence: 99%

Murein and pseudomurein cell wall binding domains of bacteria and archaea—a comparative view

Visweswaran

Dijkstra

2011

Appl Microbiol Biotechnol

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The cell wall, a major barrier protecting cells from their environment, is an essential compartment of both bacteria and archaea. It protects the organism from internal turgor pressure and gives a defined shape to the cell. The cell wall serves also as an anchoring surface for various proteins and acts as an adhesion platform for bacteriophages. The walls of bacteria and archaea are mostly composed of murein and pseudomurein, respectively. Cell wall binding domains play a crucial role in the non-covalent attachment of proteins to cell walls. Here, we give an overview of the similarities and differences in the biochemical and functional properties of the two major murein and pseudomurein cell wall binding domains, i.e., the Lysin Motif (LysM) domain (Pfam PF01476) and the pseudomurein binding (PMB) domain (Pfam PF09373) of bacteria and archaea, respectively.

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Expression of C-terminal Repeat Region of Peptidoglycan Hydrolase of Lactococcus lactis IL1403 in Methylotrophic Yeast Pichia pastoris

Cited by 13 publications

References 28 publications

Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications

Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications

Exploring Surface Display Technology for Enhancement of Delivering Viable Lactic Acid Bacteria to Gastrointestinal Tract

Murein and pseudomurein cell wall binding domains of bacteria and archaea—a comparative view

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