A5055717602- Bacterial Genetics and Biotechnology
- Bacteriophages and microbial interactions
- Escherichia coli research studies
- RNA and protein synthesis mechanisms
- Enzyme Structure and Function
- Glycosylation and Glycoproteins Research
- Legume Nitrogen Fixing Symbiosis
- Protein Structure and Dynamics
- Genomics and Phylogenetic Studies
University of Amsterdam
2020-2024
Insertion of new material into the Escherichia coli peptidoglycan (PG) sacculus between cytoplasmic membrane and outer requires a well-organized balance synthetic hydrolytic activities to maintain cell shape avoid lysis. Since most bacteria carry multiple enzymes carrying same type PG activity, we know little about specific function given enzymes. Here show that DD-carboxy/endopeptidase PBP4 localizes in PBP1A/LpoA FtsEX dependent fashion at midcell during septal synthesis. Midcell...
Balancing peptidoglycan (PG) synthesis and degradation with precision is essential for bacterial growth, yet our comprehension of this intricate process remains limited. The NlpI-Prc proteolytic complex plays a crucial but poorly understood role in the regulation multiple enzymes involved PG metabolism. In paper, through fluorescent D-amino acid 7-hydroxycoumarincarbonylamino-D-alanine (HADA) labeling immunolabeling assays, we have demonstrated that regulates activity transpeptidases...
ABSTRACT Escherichia coli has many periplasmic hydrolases to degrade and modify peptidoglycan (PG). However, the redundancy of eight PG endopeptidases makes it challenging define specific roles individual enzymes. Therefore, cellular role PBP7 (encoded by pbpG ) is not clearly defined. In this work, we show that localizes in lateral cell envelope at midcell. The C‐terminal α‐helix crucial for midcell localization but its activity, which dispensable localization. Additionally, relies on...
ABSTRACT Insertion of new material into the Escherichia coli peptidoglycan (PG) sacculus between cytoplasmic membrane and outer requires a well-organized balance synthetic hydrolytic activities to maintain cell shape avoid lysis. The enzymes outnumber that insert PG by far very little is known about their specific function. Here we show DD-carboxy/endopeptidase PBP4 localizes in PBP1A/LpoA FtsEX dependent fashion at midcell during septal synthesis. Midcell localization its non-catalytic...
The Tol-Pal proteins stabilise the outer membrane during cell division in many gram-negative bacteria, including Escherichia coli. Pal is an lipoprotein that can bind peptidoglycan. It accumulates at septum by a mobilisation-and-capture mechanism. This work further substantiates and extends knowledge of Pal's localisation E. coli using immunolabeling, this method enables detection endogenous proteins. midcell TolB, as seen with fluorescent protein fusions, division, was confirmed. retention...
The Tol-Pal proteins stabilize the outer membrane during cell division in many Gram-negative bacteria, including Escherichia coli . Pal is an lipoprotein that can bind peptidoglycan. It accumulates at septum by a mobilization-and-capture mechanism. This work further substantiates and extends knowledge of Pal’s localization E. using immunolabelling; this method enables detection endogenous proteins. midcell TolB, as seen with fluorescent protein fusions, division, was confirmed. retention...
The Tol-Pal proteins stabilise the outer membrane during cell division in many gram-negative bacteria, including Escherichia coli. Pal is an lipoprotein that can bind peptidoglycan. It accumulates at septum by a mobilisation-and-capture mechanism. This work further substantiates and extends knowledge of Pal's localisation E. coli using immunolabeling, this method enables detection endogenous proteins. midcell TolB, as seen with fluorescent protein fusions, division, was confirmed. retention...