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Journal articles on the topic 'GroESL'

Author: Grafiati

Published: 7 September 2021

Last updated: 29 July 2025

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1

Bittner, Alycia N., Amanda Foltz, and Valerie Oke. "Only One of Five groEL Genes Is Required for Viability and Successful Symbiosis in Sinorhizobium meliloti." Journal of Bacteriology 189, no. 5 (2006): 1884–89. http://dx.doi.org/10.1128/jb.01542-06.

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ABSTRACT Many bacterial species contain multiple copies of the genes that encode the chaperone GroEL and its cochaperone, GroES, including all of the fully sequenced root-nodulating bacteria that interact symbiotically with legumes to generate fixed nitrogen. In particular, in Sinorhizobium meliloti there are four groESL operons and one groEL gene. To uncover functional redundancies of these genes during growth and symbiosis, we attempted to construct strains containing all combinations of groEL mutations. Although a double groEL1 groEL2 mutant cannot be constructed, we demonstrate that the qu

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2

Bittner, Alycia N., and Valerie Oke. "Multiple groESL Operons Are Not Key Targets of RpoH1 and RpoH2 in Sinorhizobium meliloti." Journal of Bacteriology 188, no. 10 (2006): 3507–15. http://dx.doi.org/10.1128/jb.188.10.3507-3515.2006.

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ABSTRACT Among the rhizobia that establish nitrogen-fixing nodules on the roots of host plants, many contain multiple copies of genes encoding the sigma factor RpoH and the chaperone GroEL/GroES. In Sinorhizobium meliloti there are two rpoH genes, four groESL operons, and one groEL gene. rpoH1 mutants are defective for growth at high temperature and form ineffective nodules, rpoH1 rpoH2 double mutants are unable to form nodules, and groESL1 mutants form ineffective nodules. To explore the roles of RpoH1 and RpoH2, we identified mutants that suppress both the growth and nodulation defects. Thes

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3

Karunakaran, Karuna P., Yasuyuki Noguchi, Timothy D. Read, et al. "Molecular Analysis of the Multiple GroEL Proteins of Chlamydiae." Journal of Bacteriology 185, no. 6 (2003): 1958–66. http://dx.doi.org/10.1128/jb.185.6.1958-1966.2003.

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ABSTRACT Genome sequencing revealed that all six chlamydiae genomes contain three groEL-like genes (groEL1, groEL2, and groEL3). Phylogenetic analysis of groEL1, groEL2, and groEL3 indicates that these genes are likely to have been present in chlamydiae since the beginning of the lineage. Comparison of deduced amino acid sequences of the three groEL genes with those of other organisms showed high homology only for groEL1, although comparison of critical amino acid residues that are required for polypeptide binding of the Escherichia coli chaperonin GroEL revealed substantial conservation in al

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4

Chen, Hsiao-Jan, Jui-Chang Tsai, Tsung-Chain Chang, et al. "PCR-RFLP assay for species and subspecies differentiation of the Streptococcus bovis group based on groESL sequences." Journal of Medical Microbiology 57, no. 4 (2008): 432–38. http://dx.doi.org/10.1099/jmm.0.47628-0.

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The sequence diversity of groESL genes among Streptococcus bovis group isolates was analysed, including five reference strains and 36 clinical isolates. Phylogenetic analysis of the groES and groEL sequences showed that the isolates that belonged to the same species or subspecies usually clustered together. The intergenic spacer region between groES and groEL was variable in size (67–342 bp) and sequence and appeared to be a unique marker for species or subspecies determination. Sequence similarities of the groESL genes among species and subspecies ranged from 84.2 to 99.0 % in groES, and from

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5

Gahan, Cormac G. M., James O'Mahony, and Colin Hill. "Characterization of the groESL Operon inListeria monocytogenes: Utilization of Two Reporter Systems (gfp and hly) for Evaluating In Vivo Expression." Infection and Immunity 69, no. 6 (2001): 3924–32. http://dx.doi.org/10.1128/iai.69.6.3924-3932.2001.

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ABSTRACT The ability of intracellular pathogens to sense and adapt to the hostile environment of the host is an important factor governing virulence. We have sequenced the operon encoding the major heat shock proteins GroES and GroEL in the gram-positive food-borne pathogenListeria monocytogenes. The operon has a conserved orientation in the order groES groEL. Upstream ofgroES and in the opposite orientation is a gene encoding a homologue of the Bacillus subtilis protein YdiL, while downstream of groEL is a gene encoding a putative bile hydrolase. We used both reverse transcriptase-PCR (RT-PCR

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6

Susin, Michelle F., Humberto R. Perez, Regina L. Baldini, and Suely L. Gomes. "Functional and Structural Analysis of HrcA Repressor Protein from Caulobacter crescentus." Journal of Bacteriology 186, no. 20 (2004): 6759–67. http://dx.doi.org/10.1128/jb.186.20.6759-6767.2004.

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ABSTRACT A large number of bacteria regulate chaperone gene expression during heat shock by the HrcA-CIRCE system, in which the DNA element called CIRCE serves as binding site for the repressor protein HrcA under nonstress conditions. In Caulobacter crescentus, the groESL operon presents a dual type of control. Heat shock induction is controlled by a σ32-dependent promoter and the HrcA-CIRCE system plays a role in regulation of groESL expression under physiological temperatures. To study the activity of HrcA in vitro, we purified a histidine-tagged version of the protein, and specific binding

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7

Tsugawa, Hitoshi, Humie Ito, Miho Ohshima, and Yoshio Okawa. "Cell adherence-promoted activity of Plesiomonas shigelloides GroEL." Journal of Medical Microbiology 56, no. 1 (2007): 23–29. http://dx.doi.org/10.1099/jmm.0.46766-0.

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Previously, it has been demonstrated that the invasion of Caco-2 cells by Plesiomonas shigelloides induces apoptotic cell death. Therefore, the attachment to and colonization of eukaryotic intestinal host cells by P. shigelloides are important steps in causing pathogenicity. In this study, the participation of P. shigelloides GroEL in the attachment of P. shigelloides was examined. The groESL operon of P. shigelloides was isolated by PCR. The nucleotide sequence of the groESL operon of P. shigelloides revealed two ORFs of 294 nucleotides for groES and 1647 nucleotides for groEL. Cell fractiona

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8

Baldini, Regina Lúcia, Marcelo Avedissian, and Suely Lopes Gomes. "The CIRCE Element and Its Putative Repressor Control Cell Cycle Expression of the Caulobacter crescentus groESLOperon." Journal of Bacteriology 180, no. 7 (1998): 1632–41. http://dx.doi.org/10.1128/jb.180.7.1632-1641.1998.

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ABSTRACT The groESL operon is under complex regulation inCaulobacter crescentus. In addition to strong induction after exposure to heat shock, under physiological growth conditions, its expression is subject to cell cycle control. Transcription and translation of the groE genes occur primarily in predivisional cells, with very low levels of expression in stalked cells. The regulatory region of groESL contains both a ς32-like promoter and a CIRCE element. Overexpression ofC. crescentus ς32 gives rise to higher levels of GroEL and increased levels of the groESL transcript coming from the ς32-lik

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9

Inokuma, Hisashi, Kaori Fujii, Masaru Okuda, et al. "Determination of the Nucleotide Sequences of Heat Shock Operon groESL and the Citrate Synthase Gene (gltA) of Anaplasma (Ehrlichia) platys for Phylogenetic and Diagnostic Studies." Clinical and Vaccine Immunology 9, no. 5 (2002): 1132–36. http://dx.doi.org/10.1128/cdli.9.5.1132-1136.2002.

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ABSTRACT The 1,670-bp nucleotide sequence of the heat shock operon groESL and the 1,236-bp sequence of the citrate synthase gene (gltA) of Anaplasma (Ehrlichia) platys were determined. The topology of the groEL- and gltA-based phylogenetic tree was similar to that derived from 16S rRNA gene analyses with distances. Both groESL- and gltA-based PCRs specific to A. platys were also developed based upon the alignment data.

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10

Kumar, C. M. Santosh, Garima Khare, C. V. Srikanth, Anil K. Tyagi, Abhijit A. Sardesai, and Shekhar C. Mande. "Facilitated Oligomerization of Mycobacterial GroEL: Evidence for Phosphorylation-Mediated Oligomerization." Journal of Bacteriology 191, no. 21 (2009): 6525–38. http://dx.doi.org/10.1128/jb.00652-09.

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ABSTRACT The distinctive feature of the GroES-GroEL chaperonin system in mediating protein folding lies in its ability to exist in a tetradecameric state, form a central cavity, and encapsulate the substrate via the GroES lid. However, recombinant GroELs of Mycobacterium tuberculosis are unable to act as effective molecular chaperones when expressed in Escherichia coli. We demonstrate here that the inability of M. tuberculosis GroEL1 to act as a functional chaperone in E. coli can be alleviated by facilitated oligomerization. The results of directed evolution involving random DNA shuffling of

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11

Kuchanny-Ardigò, Dorota, and Barbara Lipińska. "Cloning and characterization of the groE heat-shock operon of the marine bacterium Vibrio harveyi." Microbiology 149, no. 6 (2003): 1483–92. http://dx.doi.org/10.1099/mic.0.26273-0.

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The DNA region of the Vibrio harveyi chromosome containing the heat-shock genes groES and groEL was cloned, and the genes were sequenced. These genes are arranged in the chromosome in the order groES–groEL. Northern hybridization experiments with RNA from V. harveyi and a DNA probe carrying both groES and groEL genes showed a single, heat-inducible transcript of approximately 2200 nt, indicating that these genes form an operon. Primer extension analysis revealed a strong, heat-inducible transcription start site 59 nt upstream of groES, preceded by a sequence typical for the Escherichia coli he

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12

Desmond, C., G. F. Fitzgerald, C. Stanton, and R. P. Ross. "Improved Stress Tolerance of GroESL-Overproducing Lactococcus lactis and Probiotic Lactobacillus paracasei NFBC 338." Applied and Environmental Microbiology 70, no. 10 (2004): 5929–36. http://dx.doi.org/10.1128/aem.70.10.5929-5936.2004.

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ABSTRACT The bacterial heat shock response is characterized by the elevated expression of a number of chaperone complexes. Two-dimensional polyacrylamide gel electrophoresis revealed that GroEL expression in probiotic Lactobacillus paracasei NFBC 338 was increased under heat adaptation conditions (52°C for 15 min). Subsequently, the groESL operon of L. paracasei NFBC 338 was PCR amplified, and by using the nisin-inducible expression system, two plasmids, pGRO1 and pGRO2, were constructed on the basis of vectors pNZ8048 and pMSP3535, respectively. These vectors were transferred into Lactococcus

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13

Bukliarevich, H. A., and M. A. Titok. "Role of the Structural and Functional Genes Encoding Heat Shock Proteins in Biosurfactant Synthesis by <i>Rhodococcus</i> <i>pyridinivorans</i> 5Ap." Микробиология 92, no. 4 (2023): 366–75. http://dx.doi.org/10.31857/s0026365623600049.

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Abstract—The role of groESL and dnaJ structural genes and hrcA regulatory gene, encoding the synthesis of heat shock proteins, in biosurfactant synthesis by R. pyridinivorans 5Ар was determined. The CIRCE binding sites for the regulatory protein coded by hrcA gene were revealed in the promoter regions of groESL, groEL2, and fmdB genes. GroESL and groEL2 genes expression during the late exponential phase in the medium with hexadecane at 42°C was higher than at 28°C (4.4 and 5.3 times, respectively). At the same time, no changes in expression of hrcA and fmdB genes were observed at two different

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14

Yeh, Kuo-Chen, Melicent C. Peck, and Sharon R. Long. "Luteolin and GroESL Modulate In Vitro Activity of NodD." Journal of Bacteriology 184, no. 2 (2002): 525–30. http://dx.doi.org/10.1128/jb.184.2.525-530.2002.

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ABSTRACT In the early stages of symbiosis between the soil bacterium Sinorhizobium meliloti and its leguminous host plant, alfalfa, bacterial nodulation (nod) genes are controlled by NodD1, NodD2, and NodD3, members of the LysR family of transcriptional regulators, in response to flavonoid and other inducers released by alfalfa. To gain an understanding of the biochemical aspects of this action, epitope-tagged recombinant NodD1 and NodD3 were overexpressed in Escherichia coli. The DNA binding properties of the purified recombinant NodD proteins were indistinguishable from those of NodD isolate

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15

Walker, D. Carey, Hany S. Girgis, and Todd R. Klaenhammer. "The groESL Chaperone Operon ofLactobacillus johnsonii." Applied and Environmental Microbiology 65, no. 7 (1999): 3033–41. http://dx.doi.org/10.1128/aem.65.7.3033-3041.1999.

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ABSTRACT The Lactobacillus johnsonii VPI 11088groESL operon was localized on the chromosome near the insertion element IS1223. The operon was initially cloned as a series of three overlapping PCR fragments, which were sequenced and used to design primers to amplify the entire operon. The amplified fragment was used as a probe to recover the chromosomal copy of thegroESL operon from a partial library of L. johnsonii VPI 11088 (NCK88) DNA, cloned in the shuttle vector pTRKH2. The 2,253-bp groESL fragment contained three putative open reading frames, two of which encoded the ubiquitous GroES and

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16

Corcoran, B. M., R. P. Ross, G. F. Fitzgerald, P. Dockery, and C. Stanton. "Enhanced Survival of GroESL-Overproducing Lactobacillus paracasei NFBC 338 under Stressful Conditions Induced by Drying." Applied and Environmental Microbiology 72, no. 7 (2006): 5104–7. http://dx.doi.org/10.1128/aem.02626-05.

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ABSTRACT GroESL-overproducing Lactobacillus paracasei NFBC 338 was dried, and its viability was compared with that of controls. Spray- and freeze-dried cultures overproducing GroESL exhibited ∼10-fold and 2-fold better survival, respectively, demonstrating the importance of GroESL in stress tolerance, which can be exploited to enhance the technological performance of sensitive probiotic cultures.

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17

Chaurasia, Akhilesh Kumar, and Shree Kumar Apte. "Overexpression of the groESL Operon Enhances the Heat and Salinity Stress Tolerance of the Nitrogen-Fixing Cyanobacterium Anabaena sp. Strain PCC7120." Applied and Environmental Microbiology 75, no. 18 (2009): 6008–12. http://dx.doi.org/10.1128/aem.00838-09.

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ABSTRACT The bicistronic groESL operon, encoding the Hsp60 and Hsp10 chaperonins, was cloned into an integrative expression vector, pFPN, and incorporated at an innocuous site in the Anabaena sp. strain PCC7120 genome. In the recombinant Anabaena strain, the additional groESL operon was expressed from a strong cyanobacterial P psbA1 promoter without hampering the stress-responsive expression of the native groESL operon. The net expression of the two groESL operons promoted better growth, supported the vital activities of nitrogen fixation and photosynthesis at ambient conditions, and enhanced

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18

Chai, Yunrong, and Stephen C. Winans. "The Chaperone GroESL Enhances the Accumulation of Soluble, Active TraR Protein, a Quorum-Sensing Transcription Factor from Agrobacterium tumefaciens." Journal of Bacteriology 191, no. 11 (2009): 3706–11. http://dx.doi.org/10.1128/jb.01434-08.

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ABSTRACT TraR of Agrobacterium tumefaciens is a LuxR-type quorum-sensing transcription factor that regulates genes required for replication and conjugation of the tumor-inducing (Ti) plasmid. TraR requires its cognate autoinducer N-3-oxooctanoyl-homoserine lactone (OOHL) for resistance of proteolysis in wild-type bacteria and for correct protein folding and solubility when overexpressed in E. coli. In this study, we ask whether GroESL might also play a role in TraR folding, as this molecular chaperone assists many proteins in attaining their native tertiary structure. Expression of E. coli Gro

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19

TOKUNAGA, Masao, Yoichi SHIRAISHI, Masatake ODACHI, et al. "Molecular Cloning of groESL Locus, and Purification and Characterization of Chaperonins, GroEL and GroES, from Bacillus brevis." Bioscience, Biotechnology, and Biochemistry 65, no. 6 (2001): 1379–87. http://dx.doi.org/10.1271/bbb.65.1379.

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20

Mogk, Axel, Andrea Völker, Susanne Engelmann, Michael Hecker, Wolfgang Schumann, and Uwe Völker. "Nonnative Proteins Induce Expression of the Bacillus subtilis CIRCE Regulon." Journal of Bacteriology 180, no. 11 (1998): 2895–900. http://dx.doi.org/10.1128/jb.180.11.2895-2900.1998.

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ABSTRACT The chaperone-encoding groESL and dnaKoperons constitute the CIRCE regulon of Bacillus subtilis. Both operons are under negative control of the repressor protein HrcA, which interacts with the CIRCE operator and whose activity is modulated by the GroESL chaperone machine. In this report, we demonstrate that induction of the CIRCE regulon can also be accomplished by ethanol stress and puromycin. Introduction of the hrcA gene and a transcriptional fusion under the control of the CIRCE operator intoEscherichia coli allowed induction of this fusion by heat shock, ethanol stress, and overp

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21

Schmid, Amy K., Heather A. Howell, John R. Battista, Scott N. Peterson, and Mary E. Lidstrom. "Global Transcriptional and Proteomic Analysis of the Sig1 Heat Shock Regulon of Deinococcus radiodurans." Journal of Bacteriology 187, no. 10 (2005): 3339–51. http://dx.doi.org/10.1128/jb.187.10.3339-3351.2005.

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ABSTRACT The sig1 gene, predicted to encode an extracytoplasmic function-type heat shock sigma factor of Deinococcus radiodurans, has been shown to play a central role in the positive regulation of the heat shock operons groESL and dnaKJ. To determine if Sig1 is required for the regulation of additional heat shock genes, we monitored the global transcriptional and proteomic profiles of a D. radiodurans R1 sig1 mutant and wild-type cells in response to elevated temperature stress. Thirty-one gene products were identified that showed heat shock induction in the wild type but not in the sig1 muta

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Tomas, Christopher A., Neil E. Welker, and Eleftherios T. Papoutsakis. "Overexpression of groESL in Clostridium acetobutylicum Results in Increased Solvent Production and Tolerance, Prolonged Metabolism, and Changes in the Cell's Transcriptional Program." Applied and Environmental Microbiology 69, no. 8 (2003): 4951–65. http://dx.doi.org/10.1128/aem.69.8.4951-4965.2003.

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ABSTRACT DNA array and Western analyses were used to examine the effects of groESL overexpression and host-plasmid interactions on solvent production in Clostridium acetobutylicum ATCC 824. Strain 824(pGROE1) was created to overexpress the groESL operon genes from a clostridial thiolase promoter. The growth of 824(pGROE1) was inhibited up to 85% less by a butanol challenge than that of the control strain, 824(pSOS95del). Overexpression of groESL resulted in increased final solvent titers 40% and 33% higher than those of the wild type and plasmid control strains, respectively. Active metabolism

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23

Lin, Jiusheng, and Mark A. Wilson. "Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL." Journal of Biological Chemistry 286, no. 22 (2011): 19459–69. http://dx.doi.org/10.1074/jbc.m111.238741.

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Many proteins contain a thioredoxin (Trx)-like domain fused with one or more partner domains that diversify protein function by the modular construction of new molecules. The Escherichia coli protein YbbN is a Trx-like protein that contains a C-terminal domain with low homology to tetratricopeptide repeat motifs. YbbN has been proposed to act as a chaperone or co-chaperone that aids in heat stress response and DNA synthesis. We report the crystal structure of YbbN, which is an elongated molecule with a mobile Trx domain and four atypical tetratricopeptide repeat motifs. The Trx domain lacks a

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24

Prakash, Jogadhenu S. S., Pilla Sankara Krishna, Kodru Sirisha, et al. "An RNA helicase, CrhR, regulates the low-temperature-inducible expression of heat-shock genes groES, groEL1 and groEL2 in Synechocystis sp. PCC 6803." Microbiology 156, no. 2 (2010): 442–51. http://dx.doi.org/10.1099/mic.0.031823-0.

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The crhR gene for RNA helicase, CrhR, was one of the most highly induced genes when the cyanobacterium Synechocystis sp. PCC 6803 was exposed to a downward shift in ambient temperature. Although CrhR may be involved in the acclimatization of cyanobacterial cells to low-temperature environments, its functional role during the acclimatization is not known. In the present study, we mutated the crhR gene by replacement with a spectinomycin-resistance gene cassette. The resultant ΔcrhR mutant exhibited a phenotype of slow growth at low temperatures. DNA microarray analysis of the genome-wide expres

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25

Susin, Michelle F., Regina L. Baldini, Frederico Gueiros-Filho, and Suely L. Gomes. "GroES/GroEL and DnaK/DnaJ Have Distinct Roles in Stress Responses and during Cell Cycle Progression in Caulobacter crescentus." Journal of Bacteriology 188, no. 23 (2006): 8044–53. http://dx.doi.org/10.1128/jb.00824-06.

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ABSTRACT Misfolding and aggregation of protein molecules are major threats to all living organisms. Therefore, cells have evolved quality control systems for proteins consisting of molecular chaperones and proteases, which prevent protein aggregation by either refolding or degrading misfolded proteins. DnaK/DnaJ and GroES/GroEL are the best-characterized molecular chaperone systems in bacteria. In Caulobacter crescentus these chaperone machines are the products of essential genes, which are both induced by heat shock and cell cycle regulated. In this work, we characterized the viabilities of c

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Charoenpunthuwong, Kankanok, Preekamol Klanrit, Nuttaporn Chamnipa, Sudarat Thanonkeo, Mamoru Yamada, and Pornthap Thanonkeo. "Optimization Condition for Ethanol Production from Sweet Sorghum Juice by Recombinant Zymomonas mobilis Overexpressing groESL Genes." Energies 16, no. 14 (2023): 5284. http://dx.doi.org/10.3390/en16145284.

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High-temperature ethanol fermentation (HTEF) using high-potential thermotolerant ethanologenic microorganisms is a promising platform for ethanol production in tropical or subtropical areas. This study aims to evaluate the ethanol production potential of recombinant Zymomonas mobilis R301 overexpressing groESL genes under normal and high-temperature conditions and the expression of genes involved in the heat shock response and ethanol production pathway during ethanol fermentation using sweet sorghum juice (SSJ) as feedstock. Growth characterization analysis revealed that the recombinant Z. mo

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27

Bjöersdorff, Anneli, Bodil Bagert, Robert F. Massung, Asiya Gusa, and Ingvar Eliasson. "Isolation and Characterization of Two European Strains of Ehrlichia phagocytophila of Equine Origin." Clinical and Vaccine Immunology 9, no. 2 (2002): 341–43. http://dx.doi.org/10.1128/cdli.9.2.341-343.2002.

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ABSTRACT We report the isolation and partial genetic characterization of two equine strains of granulocytic Ehrlichia of the genogroup Ehrlichia phagocytophila. Frozen whole-blood samples from two Swedish horses with laboratory-verified granulocytic ehrlichiosis were inoculated into HL-60 cell cultures. Granulocytic Ehrlichia was isolated and propagated from both horses. DNA extracts from the respective strains were amplified by PCR using primers directed towards the 16S rRNA gene, the groESL heat shock operon gene, and the ank gene. The amplified gene fragments were sequenced and compared to

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Li, Jian, Yan Wang, Cui-ying Zhang, et al. "Myxococcus xanthus Viability Depends on GroEL Supplied by Either of Two Genes, but the Paralogs Have Different Functions during Heat Shock, Predation, and Development." Journal of Bacteriology 192, no. 7 (2010): 1875–81. http://dx.doi.org/10.1128/jb.01458-09.

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ABSTRACT Myxococcus xanthus DK1622 contains two paralogous groEL gene loci that possess both different sequences and different organizations within the genome. Deletion of either one of these two genes alone does not affect cell viability. However, deletion of both groEL genes results in cell death unless a complemented groEL1 or groEL2 gene is present. The groEL1 gene was determined to be essential for cell survival under heat shock conditions; a strain with mutant groEL2 caused cells to be more sensitive than the wild-type strain to higher temperatures. Mutants with a single deletion of eith

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Musatovova, Oxana, Subramanian Dhandayuthapani, and Joel B. Baseman. "Transcriptional Heat Shock Response in the Smallest Known Self-Replicating Cell, Mycoplasma genitalium." Journal of Bacteriology 188, no. 8 (2006): 2845–55. http://dx.doi.org/10.1128/jb.188.8.2845-2855.2006.

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ABSTRACT Mycoplasma genitalium is a human bacterial pathogen linked to urethritis and other sexually transmitted diseases as well as respiratory and joint pathologies. Though its complete genome sequence is available, little is understood about the regulation of gene expression in this smallest known, self-replicating cell, as its genome lacks orthologues for most of the conventional bacterial regulators. Still, the transcriptional repressor HrcA (heat regulation at CIRCE [controlling inverted repeat of chaperone expression]) is predicted in the M. genitalium genome as well as three copies of

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Narberhaus, Franz, Michael Kowarik, Christoph Beck, and Hauke Hennecke. "Promoter Selectivity of the Bradyrhizobium japonicum RpoH Transcription Factors In Vivo and In Vitro." Journal of Bacteriology 180, no. 9 (1998): 2395–401. http://dx.doi.org/10.1128/jb.180.9.2395-2401.1998.

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ABSTRACT Expression of the dnaKJ andgroESL 1 heat shock operons ofBradyrhizobium japonicum depends on a ς32-like transcription factor. Three such factors (RpoH1, RpoH2, and RpoH3) have previously been identified in this organism. We report here that they direct transcription from some but not all ς32-type promoters when the respective rpoH genes are expressed inEscherichia coli. All three RpoH factors were purified as soluble C-terminally histidine-tagged proteins, although the bulk of overproduced RpoH3 was insoluble. The purified proteins were recognized by an anti-E. coli ς32 serum. While R

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31

Wang, Yan, Xi Li, Wenyan Zhang, Xiuwen Zhou, and Yue-zhong Li. "The groEL2 gene, but not groEL1, is required for biosynthesis of the secondary metabolite myxovirescin in Myxococcus xanthus DK1622." Microbiology 160, no. 3 (2014): 488–95. http://dx.doi.org/10.1099/mic.0.065862-0.

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Myxococcus xanthus DK1622 possesses two copies of the groEL gene: groEL1, which participates in development, and groEL2, which is involved in the predatory ability of cells. In this study, we determined that the groEL2 gene is required for the biosynthesis of the secondary metabolite myxovirescin (TA), which plays essential roles in predation. The groEL2-knockout mutant strain was defective in producing a zone of inhibition and displayed decreased killing ability against Escherichia coli, while the groEL1-knockout mutant strain exhibited little difference from the wild-type strain DK1622. HPLC

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Kim, Dong-Gyun, Yu-Ri Kim, Eun-Young Kim, Hyun Min Cho, Sun-Hee Ahn, and In-Soo Kong. "Isolation of the groESL cluster from Vibrio anguillarum and PCR detection targeting groEL gene." Fisheries Science 76, no. 5 (2010): 803–10. http://dx.doi.org/10.1007/s12562-010-0266-y.

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Schmid, Amy K., and Mary E. Lidstrom. "Involvement of Two Putative Alternative Sigma Factors in Stress Response of the Radioresistant Bacterium Deinococcus radiodurans." Journal of Bacteriology 184, no. 22 (2002): 6182–89. http://dx.doi.org/10.1128/jb.184.22.6182-6189.2002.

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ABSTRACT Two genes bearing similarity to alternative sigma factors were identified in the Deinococcus radiodurans genome sequence and designated sig1 and sig2. These genes were cloned and inactivated, and both were found to be important for survival during heat and ethanol stress, although the sig1 mutants displayed a more severe phenotype than the sig2 mutants. Reporter gene fusions to the groESL and dnaKJ operons transformed into these mutant backgrounds indicated that sig1 is required for the heat shock induction of groESL and dnaKJ, whereas sig2 mutants show a more moderate defect in dnaKJ

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Roncarati, Davide, Alberto Danielli, Gunther Spohn, Isabel Delany, and Vincenzo Scarlato. "Transcriptional Regulation of Stress Response and Motility Functions in Helicobacter pylori Is Mediated by HspR and HrcA." Journal of Bacteriology 189, no. 20 (2007): 7234–43. http://dx.doi.org/10.1128/jb.00626-07.

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ABSTRACT The hrcA and hspR genes of Helicobacter pylori encode two transcriptional repressor proteins that negatively regulate expression of the groES-groEL and hrcA-grpE-dnaK operons. While HspR was previously shown to bind far upstream of the promoters transcribing these operons, the binding sites of HrcA were not identified. Here, we demonstrate by footprinting analysis that HrcA binds to operator elements similar to the so-called CIRCE sequences overlapping both promoters. Binding of HspR and HrcA to their respective operators occurs in an independent manner, but the DNA binding activity o

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Lemos, José A. C., Yi-Ywan M. Chen, and Robert A. Burne. "Genetic and Physiologic Analysis of thegroE Operon and Role of the HrcA Repressor in Stress Gene Regulation and Acid Tolerance in Streptococcus mutans." Journal of Bacteriology 183, no. 20 (2001): 6074–84. http://dx.doi.org/10.1128/jb.183.20.6074-6084.2001.

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ABSTRACT Our working hypothesis is that the major molecular chaperones DnaK and GroE play central roles in the ability of oral bacteria to cope with the rapid and frequent stresses encountered in oral biofilms, such as acidification and nutrient limitation. Previously, our laboratory partially characterized the dnaK operon ofStreptococcus mutans(hrcA-grpE-dnaK) and demonstrated that dnaK is up-regulated in response to acid shock and sustained acidification (G. C. Jayaraman, J. E. Penders, and R. A. Burne, Mol. Microbiol. 25:329–341, 1997). Here, we show that thegroESL genes of S. mutans consti

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Broadbent, J. R., C. J. Oberg, and L. Wei. "Characterization of the Lactobacillus helveticus groESL operon." Research in Microbiology 149, no. 4 (1998): 247–53. http://dx.doi.org/10.1016/s0923-2508(98)80300-8.

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Lee, W. T., K. C. Terlesky, and F. R. Tabita. "Cloning and characterization of two groESL operons of Rhodobacter sphaeroides: transcriptional regulation of the heat-induced groESL operon." Journal of bacteriology 179, no. 2 (1997): 487–95. http://dx.doi.org/10.1128/jb.179.2.487-495.1997.

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Taguchi, Hideki, Keigo Tsukuda, Fumihiro Motojima, Ayumi Koike-Takeshita, and Masasuke Yoshida. "BeFxStops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers." Journal of Biological Chemistry 279, no. 44 (2004): 45737–43. http://dx.doi.org/10.1074/jbc.m406795200.

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Coupling with ATP hydrolysis and cooperating with GroES, the double ring chaperonin GroEL assists the folding of other proteins. Here we report novel GroEL-GroES complexes formed in fluoroberyllate (BeFx) that can mimic the phosphate part of the enzyme-bound nucleotides. In ATP, BeFxstops the functional turnover of GroEL by preventing GroES release and produces a symmetric 1:2 GroEL-GroES complex in which both GroEL rings contain ADP·BeFxand an encapsulated substrate protein. In ADP, the substrate protein-loaded GroEL cannot bind GroES. In ADPplusBeFx, however, it can bind GroES to form a stab

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MALMSTEN, J., D. GAVIER WIDÉN, G. RYDEVIK, et al. "Temporal and spatial variation in Anaplasma phagocytophilum infection in Swedish moose (Alces alces)." Epidemiology and Infection 142, no. 6 (2013): 1205–13. http://dx.doi.org/10.1017/s0950268813002094.

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SUMMARYThe occurrence of Anaplasma phagocytophilum was investigated in spleen and serum samples from Swedish moose (Alces alces) in southern Sweden (island and mainland). Samples were analysed for presence of A. phagocytophilum DNA by real-time PCR (n = 263), and for Anaplasma antibodies with ELISA serology (n = 234). All serum samples had antibodies against A. phagocytophilum. The mean DNA-based prevalence was 26·3%, and significant (P < 0·01) temporal, and spatial variation was found. Island moose had significantly (P < 0·001) higher prevalence of A. phagocytophilum DNA than moose from

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Tauschek, Marija, Christopher W. Hamilton, Leslie A. Hall, Chariya Chomvarin, Janet A. M. Fyfe, and John K. Davies. "Transcriptional analysis of the groESL operon of Neisseriagonorrhoeae." Gene 189, no. 1 (1997): 107–12. http://dx.doi.org/10.1016/s0378-1119(96)00842-6.

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de Leon, P., S. Marco, C. Isiegas, A. Marina, J. L. Carrascosa, and R. P. Mellado. "Streptomyces lividans groES, groEL1 and groEL2 genes." Microbiology 143, no. 11 (1997): 3563–71. http://dx.doi.org/10.1099/00221287-143-11-3563.

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Ventura, Marco, Carlos Canchaya, Ralf Zink, Gerald F. Fitzgerald, and Douwe van Sinderen. "Characterization of the groEL and groES Loci in Bifidobacterium breve UCC 2003: Genetic, Transcriptional, and Phylogenetic Analyses." Applied and Environmental Microbiology 70, no. 10 (2004): 6197–209. http://dx.doi.org/10.1128/aem.70.10.6197-6209.2004.

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ABSTRACT The bacterial heat shock response is characterized by the elevated expression of a number of chaperone complexes, including the GroEL and GroES proteins. The groES and groEL genes are highly conserved among eubacteria and are typically arranged as an operon. Genome analysis of Bifidobacterium breve UCC 2003 revealed that the groES and groEL genes are located in different chromosomal regions. The heat inducibility of the groEL and groES genes of B. breve UCC 2003 was verified by slot blot analysis. Northern blot analyses showed that the cspA gene is cotranscribed with the groEL gene, w

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Hotokezaka, H., N. Ohara, H. Hayashida, et al. "Transcriptional analysis of the groESL operon from Porphyromonas gingivalis." Oral Microbiology and Immunology 12, no. 4 (1997): 236–39. http://dx.doi.org/10.1111/j.1399-302x.1997.tb00385.x.

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Hung, Wei-Chung, Jui-Chang Tsai, Po-Ren Hsueh, Jean-San Chia, and Lee-Jene Teng. "Species identification of mutans streptococci by groESL gene sequence." Journal of Medical Microbiology 54, no. 9 (2005): 857–62. http://dx.doi.org/10.1099/jmm.0.46180-0.

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Akiko, Okamoto-Kainuma, Yan Wang, Kadono Sachiko, Tayama Kenji, Koizumi Yukimichi, and Yanagida Fujiharu. "Cloning and Characterization of groESL Operon in Acetobacter aceti." Journal of Bioscience and Bioengineering 94, no. 2 (2002): 140–47. http://dx.doi.org/10.1016/s1389-1723(02)80134-7.

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OKAMOTO-KAINUMA, AKIKO, YAN WANG, SACHIKO KADONO, KENJI TAYAMA, YUKIMICHI KOIZUMI, and FUJIHARU YANAGIDA. "Cloning and Characterization of groESL Operon in Acetobacter aceti." Journal of Bioscience and Bioengineering 94, no. 2 (2002): 140–47. http://dx.doi.org/10.1263/jbb.94.140.

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Noshiro, Daisuke, and Toshio Ando. "Substrate protein dependence of GroEL–GroES interaction cycle revealed by high-speed atomic force microscopy imaging." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1749 (2018): 20170180. http://dx.doi.org/10.1098/rstb.2017.0180.

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A double-ring-shaped tetradecameric GroEL complex assists proper protein folding in cooperation with the cochaperonin GroES. The dynamic GroEL–GroES interaction reflects the allosteric intra- and inter-ring communications and the chaperonin reaction. Therefore, revealing this dynamic interaction is essential to understanding the allosteric communications and the operation mechanism of GroEL. Nevertheless, how this interaction proceeds in the chaperonin cycle has long been controversial. Here, we directly image the dynamic GroEL–GroES interaction under conditions with and without foldable subst

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Green, Heather A., and Timothy J. Donohue. "Activity of Rhodobacter sphaeroides RpoHII, a Second Member of the Heat Shock Sigma Factor Family." Journal of Bacteriology 188, no. 16 (2006): 5712–21. http://dx.doi.org/10.1128/jb.00405-06.

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ABSTRACT We have identified a second RpoH homolog, RpoHII, in the α-proteobacterium Rhodobacter sphaeroides. Primary amino acid sequence comparisons demonstrate that R. sphaeroides RpoHII belongs to a phylogenetically distinct group with RpoH orthologs from α-proteobacteria that contain two rpoH genes. Like its previously identified paralog, RpoHI, RpoHII is able to complement the temperature-sensitive phenotype of an Escherichia coli σ32 (rpoH) mutant. In addition, we show that recombinant RpoHI and RpoHII each transcribe two E. coli σ32-dependent promoters (rpoD PHS and dnaK P1) when reconst

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Spohn, Gunther, Alberto Danielli, Davide Roncarati, Isabel Delany, Rino Rappuoli, and Vincenzo Scarlato. "Dual Control of Helicobacter pylori Heat Shock Gene Transcription by HspR and HrcA." Journal of Bacteriology 186, no. 10 (2004): 2956–65. http://dx.doi.org/10.1128/jb.186.10.2956-2965.2004.

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ABSTRACT The HspR repressor regulates transcription of the groESL, hrcA-grpE-dnaK, and cbpA-hspR-orf operons of Helicobacter pylori. Here we show that two of the HspR-regulated operons, namely, the groESL and dnaK operons, encoding the major cellular chaperone machineries are also regulated by the H. pylori homologue of the HrcA repressor. Similarly to the hspR mutation, deletion of the hrcA gene also leads to complete derepression of the P gro and P hrc promoters. The presence of both HspR and HrcA is therefore necessary for regulated transcription from these promoters. HrcA binds directly to

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Tran, Huyen-Thi, Jongha Lee, Hyunjae Park, et al. "Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae." Crystals 9, no. 8 (2019): 399. http://dx.doi.org/10.3390/cryst9080399.

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Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen that causes bacterial blight of rice, with outbreaks occurring in most rice-growing countries. Thus far, there is no effective pesticide against bacterial blight. Chaperones in bacterial pathogens are important for the stabilization and delivery of effectors into host cells to cause disease. In bacteria, GroEL/GroES complex mediates protein folding and protects proteins against misfolding and aggregation caused by environmental stress. We determined the crystal structure of GroEL from Xanthomonas oryzae pv. oryzae (XoGroEL) at 3.2 Å resol

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