Faculty Opinions recommendation of Transcription facilitated genome-wide recruitment of topoisomerase I and DNA gyrase.

2017 ◽  
Author(s):  
Charles Dorman
Keyword(s):  
Topoisomerase I ◽  
Dna Gyrase ◽  
Genome Wide

scholarly journals Transcription facilitated genome-wide recruitment of topoisomerase I and DNA gyrase

PLoS Genetics ◽  
2017 ◽  
Vol 13 (5) ◽  
pp. e1006754 ◽  
Author(s):  
Wareed Ahmed ◽  
Claudia Sala ◽  
Shubhada R. Hegde ◽  
Rajiv Kumar Jha ◽  
Stewart T. Cole ◽  
...  
Keyword(s):  
Topoisomerase I ◽  
Dna Gyrase ◽  
Genome Wide

scholarly journals Metabolic Engineering for l-Glutamine Overproduction by Using DNA Gyrase Mutations in Escherichia coli

2013 ◽  
Vol 79 (9) ◽  
pp. 3033-3039 ◽  
Author(s):  
Mikiro Hayashi ◽  
Kazuhiko Tabata
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Topoisomerase I ◽  
Dna Gyrase ◽  
Chromosomal Dna ◽  
Topoisomerase Iv ◽  
Α Subunit ◽  
Content Type ◽  
Genome Wide ◽  
K 12

ABSTRACTAnl-glutamine-overproducing mutant of anEscherichia coliK-12-derived strain was selected from randomly mutagenized cells in the course ofl-alanyl-l-glutamine strain development. Genome-wide mutation analysis unveiled a novel mechanism forl-glutamine overproduction in this mutant. Three mutations were identified that are related to thel-glutamine overproduction phenotype, namely, an intergenic mutation in the 5′-flanking region ofyeiGand two nonsynonymous mutations ingyrA(Gly821Ser and Asp830Asn). Expression ofyeiG, which encodes a putative esterase, was enhanced by the intergenic mutation. The nonsynonymous mutations ingyrA, a gene that encodes the DNA gyrase α subunit, affected the DNA topology of the cells. Gyrase is a type II topoisomerase that adds negative supercoils to double-stranded DNA. When the opposing DNA-relaxing activity was enhanced by overexpressing topoisomerase I (topA) and topoisomerase IV (parCandparE), an increase inl-glutamine production was observed. These results indicate that a reduction of chromosomal DNA supercoils in the mutant caused an increase inl-glutamine accumulation. The mechanism underlying this finding is discussed in this paper. We also constructed anl-glutamine-hyperproducing strain by attenuating cellularl-glutamine degradation activity. Although the reconstituted mutant (withyeiGtogether withgyrA) produced 200 mMl-glutamine, metabolic engineering finally enabled construction of a mutant that accumulated more than 500 mMl-glutamine.

scholarly journals Effects of DNA gyrase inhibitors in Escherichia coli topoisomerase I mutants.

1986 ◽  
Vol 168 (1) ◽  
pp. 276-282 ◽  
Author(s):  
G J Pruss ◽  
R J Franco ◽  
S G Chevalier ◽  
S H Manes ◽  
K Drlica
Keyword(s):  
Escherichia Coli ◽  
Topoisomerase I ◽  
Dna Gyrase ◽  
Gyrase Inhibitors

scholarly journals Nonclassic Functions of Human Topoisomerase I: Genome-Wide and Pharmacologic Analyses

2007 ◽  
Vol 67 (18) ◽  
pp. 8752-8761 ◽  
Author(s):  
Ze-Hong Miao ◽  
Audrey Player ◽  
Uma Shankavaram ◽  
Yong-Hong Wang ◽  
Drazen B. Zimonjic ◽  
...  
Keyword(s):  
Topoisomerase I ◽  
Genome Wide

gyrB-225, a mutation of DNA gyrase that compensates for topoisomerase I deficiency: investigation of its low activity and quinolone hypersensitivity

2001 ◽  
Vol 309 (5) ◽  
pp. 1219-1231 ◽  
Author(s):  
Jonathan G Heddle ◽  
Tao Lu ◽  
Xilin Zhao ◽  
Karl Drlica ◽  
Anthony Maxwell
Keyword(s):  
Topoisomerase I ◽  
Dna Gyrase ◽  
Low Activity

scholarly journals Structural Maintenance of Chromosomes Protein of Bacillussubtilis Affects Supercoiling In Vivo

2002 ◽  
Vol 184 (19) ◽  
pp. 5317-5322 ◽  
Author(s):  
Janet C. Lindow ◽  
Robert A. Britton ◽  
Alan D. Grossman
Keyword(s):  
Topoisomerase I ◽  
Dna Gyrase ◽  
Dna Supercoiling ◽  
Null Mutant ◽  
Wild Type ◽  
Mutant Plasmid ◽  
Chromatid Cohesion ◽  
Structural Maintenance Of Chromosomes ◽  
Gyrase Inhibitors

ABSTRACT Structural maintenance of chromosomes (SMC) proteins are found in nearly all organisms. Members of this protein family are involved in chromosome condensation and sister chromatid cohesion. Bacillus subtilis SMC protein (BsSMC) plays a role in chromosome organization and partitioning. To better understand the function of BsSMC, we studied the effects of an smc null mutation on DNA supercoiling in vivo. We found that an smc null mutant was hypersensitive to the DNA gyrase inhibitors coumermycin A1 and norfloxacin. Furthermore, depleting cells of topoisomerase I substantially suppressed the partitioning defect of an smc null mutant. Plasmid DNA isolated from an smc null mutant was more negatively supercoiled than that from wild-type cells. In vivo cross-linking experiments indicated that BsSMC was bound to the plasmid. Our results indicate that BsSMC affects supercoiling in vivo, most likely by constraining positive supercoils, an activity which contributes to chromosome compaction and organization.

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