Biochemical and Biophysical Research Communications
Regular ArticleIdentification of Two Penicillin-Binding Multienzyme Complexes in Haemophilus influenzae
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2011, Seminars in Cell and Developmental BiologyCitation Excerpt :Upon cell division, growth shifts to the midcell division site, or septum, to generate the nascent poles. The composition and location of the peptidoglycan synthesis and remodeling machinery shift to organize around the well-studied septal FtsZ ring [14,16–19] (Fig. 1). This highly conserved machinery governs division even in spherical bacteria, with local peptidoglycan incorporation at the FtsZ ring despite the fully spherical morphological symmetry of the resulting daughters [20–23].
Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
2010, CellCitation Excerpt :Prior genetic studies indicated that cells remain viable if either PBP1a or PBP1b is inactivated, but not if they both are (Yousif et al., 1985; Kato et al., 1985). This suggests that there are at least two major PG-synthesizing complexes in the cell, one containing PBP1a and the other PBP1b, an idea supported by crosslinking studies in Haemophilus influenzae and immunoprecipitation studies in E. coli (Charpentier et al., 2002; Alaedini and Day, 1999). Based on this, we reasoned that we could identify critical components of these multienzyme PBP complexes by performing a screen for mutations synthetically lethal with the loss of either PBP1a or PBP1b.
Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation
2010, Journal of Molecular BiologyMurein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
2008, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :In Enterococcus faecalis, β-lactam resistance is mediated by PBP5 (class B) only if PBPF (class A) is active [142]. Cross-linking of proteins in H. influenzae cells revealed the existence of two different high-molecular-weight complexes containing class A and class B PBPs [143]. And finally, in C. crescentus several PBPs, probably PBP1a, PBP2a, PBP2b and PBP3a, co-immunoprecipitated with PBP2 [144].
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