Results 161 to 170 of about 2,281 (190)
Genetic Analysis of the Cell Division Protein FtsI (PBP3): Amino Acid Substitutions That Impair Septal Localization of FtsI and Recruitment of FtsN [PDF]
Journal of Bacteriology, 2004 ABSTRACT FtsI (also called PBP3) of Escherichia coli is a transpeptidase required for synthesis of peptidoglycan in the division septum and is one of several proteins that localize to the septal ring.
David S Weiss
exaly +3 more sources
Role of inter-species recombination of the ftsI gene in the dissemination of altered penicillin-binding-protein-3-mediated resistance in Haemophilus influenzae and Haemophilus haemolyticus [PDF]
Journal of Antimicrobial Chemotherapy, 2014 Objectives: To screen the ftsI gene sequences obtained from clinical isolates of non-typeable H. influenzae (NTHi), and Haemophilus haemolyticus for the presence of mosaic ftsI gene structures, and to evaluate the role homologous recombination of the ...
Elizabeth A Witherden +2 more
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Escherichia coli mutant Y16 is a double mutant carrying thermosensitive ftsH and ftsI mutations
Journal of Bacteriology, 1992 The Escherichia coli mutant Y16, which shows thermosensitive colony formation and filamentation with reduced amounts of penicillin-binding protein 3 (PBP3), has mutations in the ftsI gene encoding PBP3 and in the ftsH gene. The ftsI mutation markedly reduces the amount of PBP3 at 42 degrees C, whereas the amount of the ftsH single mutant is slightly ...
K J Begg, T Tomoyasu, W D Donachie
exaly +4 more sources
Archives of Microbiology, 2022 Abstract Haemophilus influenzae is causative agent of serious infections especially among children. β-lactam antibiotics are commonly used for treatment of these infections. Among H. influenzae isolates, β-lactam resistance can be due to the presence of either a β-lactamase, or in β-lactamase negative ampicillin resistant strains (BLNAR), to ...
Stephen Tristram, Bulent Bozdogan
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Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL [PDF]
Journal of Bacteriology, 1999 ABSTRACT Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of Escherichia coli , consists of a short cytoplasmic domain, a single membrane-spanning segment, and a large periplasmic ...
David S Weiss +2 more
exaly +3 more sources
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The essential domain of FtsN triggers cell division by promoting interaction between FtsL and FtsI
2023Abstract Cell division in bacteria requires the activation of FtsWI at the division site to synthesize septal peptidoglycan. In E. coli FtsN activates FtsWI and a previous model posited that the essential domain of FtsN ( E FtsN) acts on FtsQLB ...
Kyung-Tae Park +4 more
openaire +1 more source
Optics Letters, 2007
A novel Fourier transform spectral interferometric (FTSI) multiplex coherent anti-Stokes Raman scattering (CARS) technique is developed to extract the vibrational spectrum equivalent to the spontaneous Raman scattering. The conventional FTSI method is modified to use the internal nonresonant CARS signal as a local oscillator to perform spectral ...
Sang-Hyun Lim, Stephen R Leone
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A novel Fourier transform spectral interferometric (FTSI) multiplex coherent anti-Stokes Raman scattering (CARS) technique is developed to extract the vibrational spectrum equivalent to the spontaneous Raman scattering. The conventional FTSI method is modified to use the internal nonresonant CARS signal as a local oscillator to perform spectral ...
Sang-Hyun Lim, Stephen R Leone
exaly +3 more sources
Isolation of ftsI and murE genes involved in peptidoglycan synthesis from Corynebacterium glutamicum
Applied Microbiology and Biotechnology, 2001Corynebacterium glutamicum is known to excrete large amounts of L-glutamic acid upon treatment by penicillin. However, the mechanism of L-glutamate overproduction by penicillin treatment is still unknown. A 5.3-kb HindIII fragment was isolated by directly introducing the C.
Wijayarathna, C. D. +2 more
openaire +2 more sources