scholarly journals Further studies on rod A mutant: A round morphological mutant of Escherichia coli K-12 with wild-type penicillin-binding protein 2.

1980 ◽  
Vol 44 (12) ◽  
pp. 2937-2941 ◽  
Author(s):  
Hiroshi MATSUZAWA ◽  
Sadamitsu ASOH ◽  
Takahisa OHTA ◽  
Shigeo TAMAKI ◽  
Michio MATSUHASHI
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Morphological Mutant ◽  
K 12

scholarly journals Penicillin-Binding Protein-Related Factor A Is Required for Proper Chromosome Segregation in Bacillus subtilis

2000 ◽  
Vol 182 (6) ◽  
pp. 1650-1658 ◽  
Author(s):  
Lotte B. Pedersen ◽  
Peter Setlow
Keyword(s):  
Escherichia Coli ◽  
Chromosome Segregation ◽  
Basic Protein ◽  
Binding Protein ◽  
Related Factor ◽  
Penicillin Binding Protein ◽  
Rich Medium ◽  
Wild Type ◽  
Gene Encoding ◽  
Mutant Cells

ABSTRACT Previous work has shown that the ponA gene, encoding penicillin-binding protein 1 (PBP1), is in a two-gene operon withprfA (PBP-related factor A) (also called recU), which encodes a putative 206-residue basic protein (pI = 10.1) with no significant sequence homology to proteins with known functions. Inactivation of prfA results in cells that grow slower and vary significantly in length relative to wild-type cells. We now show that prfA mutant cells have a defect in chromosome segregation resulting in the production of ∼0.9 to 3% anucleate cells in prfA cultures grown at 30 or 37°C in rich medium and that the lack of PrfA exacerbates the chromosome segregation defect in smc and spoOJ mutant cells. In addition, overexpression of prfA was found to be toxic for and cause nucleoid condensation in Escherichia coli.

scholarly journals Deletion of the yiaMNO transporter genes affects the growth characteristics of Escherichia coli K-12

Microbiology ◽  
2005 ◽  
Vol 151 (5) ◽  
pp. 1683-1689 ◽  
Author(s):  
Titia H. Plantinga ◽  
Chris van der Does ◽  
Danuta Tomkiewicz ◽  
Geertje van Keulen ◽  
Wil N. Konings ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Biofilm Formation ◽  
Sole Carbon Source ◽  
Binding Protein ◽  
Physiological Role ◽  
Proton Motive Force ◽  
Growth Characteristics ◽  
Wild Type ◽  
E Coli ◽  
K 12

Binding-protein-dependent secondary transporters make up a unique transport protein family. They use a solute-binding protein in proton-motive-force-driven transport. Only a few systems have been functionally analysed. The yiaMNO genes of Escherichia coli K-12 encode one family member that transports the rare pentose l-xylulose. Its physiological role is unknown, since wild-type E. coli K-12 does not utilize l-xylulose as sole carbon source. Deletion of the yiaMNO genes in E. coli K-12 strain MC4100 resulted in remarkable changes in the transition from exponential growth to the stationary phase, high-salt survival and biofilm formation.

In vitro peptidoglycan polymerization catalysed by penicillin binding protein 1b of Escherichia coli K-12

FEBS Letters ◽  
1980 ◽  
Vol 110 (2) ◽  
pp. 245-249 ◽  
Author(s):  
Hideho Suzuki ◽  
Yveline Van Heijenoort ◽  
Toshihide Tamura ◽  
Junzo Mizoguchi ◽  
Yukinori Hirota ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
K 12

scholarly journals Penicillin-binding protein 2 is essential in wild-type Escherichia coli but not in lov or cya mutants.

1989 ◽  
Vol 171 (6) ◽  
pp. 3025-3030 ◽  
Author(s):  
T Ogura ◽  
P Bouloc ◽  
H Niki ◽  
R D'Ari ◽  
S Hiraga ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Wild Type

scholarly journals Differential Suppression of priA2::kan Phenotypes in Escherichia coli K-12 by Mutations in priA, lexA, and dnaC

Genetics ◽  
1996 ◽  
Vol 143 (1) ◽  
pp. 5-13 ◽  
Author(s):  
Steven J Sandler ◽  
Hardeep S Samra ◽  
Alvin J Clark
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Mutant Allele ◽  
Wild Type ◽  
Suppressor Mutations ◽  
Dnab Helicase ◽  
K 12 ◽  
Extragenic Suppressors ◽  
Assembly Activity

Abstract First identified as an essential component of the ϕX174 in vitro DNA replication system, PriA has ATPase, helicase, translocase, and primosome-assembly activities. priA1::kan strains of Escherichia coli are sensitive to UV irradiation, deficient in homologous recombination following transduction, and filamentous. priA2::kan strains have eightfold higher levels of uninduced SOS expression than wild type. We show that (1) priA1::kan strains have eightfold higher levels of uninduced SOS expression, (2) priA2::kan strains are UVS and Rec−, (3) lexA3 suppresses the high basal levels of SOS expression of a priA2::kan strain, and (4) plasmid-encoded priA300 (K230R), a mutant allele retaining only the primosome-assembly activity of priA+, restores both UVR and Rec+ phenotypes to a priA2::kan strain. Finally, we have isolated 17 independent UVR Rec+ revertants of priA2::kan strains that carry extragenic suppressors. All 17 map in the C-terminal half of the dnaC gene. DnaC loads the DnaB helicase onto DNA as a prelude for primosome assembly and DNA replication. We conclude that priA's primosome-assembly activity is essential for DNA repair and recombination and that the dnaC suppressor mutations allow these processes to occur in the absence of priA.

Sign in / Sign up

Export Citation Format

Share Document