Biotechnologically relevant enzymes and proteins

Applied Microbiology and Biotechnology

, Volume 96, Issue 3, pp 729-737

First online:

Open Access This content is freely available online to anyone, anywhere at any time.

A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material

  • Ganesh Ram R. VisweswaranAffiliated withDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of GroningenLaboratory of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen
  • , Bauke W. DijkstraAffiliated withLaboratory of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen
  • , Jan KokAffiliated withDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen Email author 

Abstract

The major murein and pseudomurein cell wall-binding domains, i.e., the Lysin Motif (LysM) (Pfam PF01476) and pseudomurein cell wall-binding (PMB) (Pfam PF09373) motif, respectively, were genetically fused. The fusion protein is capable of binding to both murein- and pseudomurein-containing cell walls. In addition, it also binds to chitin, the major polymer of fungal cell walls. Binding is influenced by pH and occurs at a pH close to the pI of the binding protein. Functional studies on truncated versions of the fusion protein revealed that murein and chitin binding is provided by the LysM domain, while binding to pseudomurein is achieved through the PMB domain.

Keywords

Murein Pseudomurein Chitin Domain