groEL expression in gyrB mutants of Borrelia burgdorferi. 2002

Janet Alverson, and D Scott Samuels
Division of Biological Sciences, The University of Montana, Missoula, Montana 59812, USA. janalverson@msa-msstate.ars.usda.gov

GroEL protein and groEL mRNA transcript were up-regulated in gyrB mutants of Borrelia burgdorferi, a causative agent of Lyme disease. Furthermore, the protein and transcript levels in gyrB mutants were greater than those in experimentally heat-shocked cultures of wild-type B. burgdorferi. Circular DNA in the gyrB mutants was more relaxed than in wild-type cells, although groEL is on the linear chromosome of B. burgdorferi. To our knowledge, this is the first evidence, albeit indirect, for the effect of DNA topology on gene expression from a linear DNA molecule in a bacterium.

UI MeSH Term Description Entries
D009690 Nucleic Acid Conformation The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape. DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D003374 Coumarins Synthetic or naturally occurring substances related to coumarin, the delta-lactone of coumarinic acid. 1,2-Benzopyrone Derivatives,1,2-Benzopyrones,Coumarin Derivative,Coumarine,1,2-Benzo-Pyrones,Benzopyran-2-ones,Coumarin Derivatives,Coumarines,1,2 Benzo Pyrones,1,2 Benzopyrone Derivatives,1,2 Benzopyrones,Benzopyran 2 ones,Derivative, Coumarin,Derivatives, 1,2-Benzopyrone,Derivatives, Coumarin
D015854 Up-Regulation A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins. Receptor Up-Regulation,Upregulation,Up-Regulation (Physiology),Up Regulation
D015964 Gene Expression Regulation, Bacterial Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria. Bacterial Gene Expression Regulation,Regulation of Gene Expression, Bacterial,Regulation, Gene Expression, Bacterial
D049933 Aminocoumarins COUMARINS with an amino group, exemplified by NOVOBIOCIN. Amino-Coumarins,Amino Coumarins
D059005 Topoisomerase II Inhibitors Compounds that inhibit the activity of DNA TOPOISOMERASE II. Included in this category are a variety of ANTINEOPLASTIC AGENTS which target the eukaryotic form of topoisomerase II and ANTIBACTERIAL AGENTS which target the prokaryotic form of topoisomerase II. DNA Gyrase Inhibitor,DNA Topoisomerase II Inhibitor,Topoisomerase 2 Inhibitors,Topoisomerase II Inhibitor,DNA Gyrase Inhibitors,DNA Topoisomerase II Inhibitors,DNA Type 2 Topoisomerase Inhibitors,Gyrase Inhibitor, DNA,Gyrase Inhibitors, DNA,II Inhibitor, Topoisomerase,Inhibitor, DNA Gyrase,Inhibitor, Topoisomerase II,Inhibitors, DNA Gyrase,Inhibitors, Topoisomerase 2,Inhibitors, Topoisomerase II
D018834 Chaperonin 60 A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein. Heat-Shock Proteins 60,hsp60 Family,GroEL Protein,GroEL Stress Protein,Heat-Shock Protein 60,hsp60 Protein,Heat Shock Protein 60,Heat Shock Proteins 60
D025065 Borrelia burgdorferi A specific species of bacteria, part of the BORRELIA BURGDORFERI GROUP, whose common name is Lyme disease spirochete. Borrelia burgdorferi sensu stricto,Lyme Disease Spirochete
D027081 DNA Gyrase A bacterial DNA topoisomerase II that catalyzes ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. Gyrase binds to DNA as a heterotetramer consisting of two A and two B subunits. In the presence of ATP, gyrase is able to convert the relaxed circular DNA duplex into a superhelix. In the absence of ATP, supercoiled DNA is relaxed by DNA gyrase. DNA Gyrase A Subunit,DNA Gyrase B Subunit,DNA-Gyrase,GyrA Protein,GyrB Protein

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