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M re B and M ur G as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis
Author(s) -
FaviniStabile Sandy,
ContrerasMartel Carlos,
Thielens Nicole,
Dessen Andréa
Publication year - 2013
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.12171
Subject(s) - peptidoglycan , periplasmic space , biosynthesis , cytoplasm , biology , biochemistry , enzyme , escherichia coli , gene
Summary Peptidoglycan is a major determinant of cell shape in bacteria, and its biosynthesis involves the concerted action of cytoplasmic, membrane‐associated and periplasmic enzymes. Within the cytoplasm, M ur enzymes catalyse the first steps leading to peptidoglycan precursor biosynthesis, and have been suggested as being part of a multicomponent complex that could also involve the transglycosylase M ur G and the cytoskeletal protein M re B . In order to initialize the characterization of a potential M ur interaction network, we purified M ur D , M ur E , M ur F , M ur G and M re B from T hermotoga maritima and characterized their interactions using membrane blotting and surface plasmon resonance. M ur D , M ur E and M ur F all recognize M ur G and M re B , but not each other, while the two latter proteins interact. In addition, we solved the crystal structures of M ur D , M ur E and M ur F , which indicate that their C ‐termini display high conformational flexibilities. The differences in M ur conformations could be important parameters for the stability of an intracytoplasmic murein biosynthesis complex.