Search Results - "KERN, Renée"

The Chemical Chaperone Proline Relieves the Thermosensitivity of a dnaK Deletion Mutant at 42°C by CHATTOPADHYAY, Madhab K, KERN, Renée, MISTOU, Michel-Yves, DANDEKAR, Abhaya M, URATSU, Sandra L, RICHARME, Gilbert

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Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase by Kern, Renée, Malki, Abderrahim, Holmgren, Arne, Richarme, Gilbert

“…Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that…”
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Peptidase Activity of the Escherichia coli Hsp31 Chaperone by Malki, Abderrahim, Caldas, Thérèse, Abdallah, Jad, Kern, Renée, Eckey, Viola, Kim, So Jung, Cha, Sun-Shin, Mori, Hirotada, Richarme, Gilbert

“…Hsp31, the Escherichia coli hcha gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperature. Its crystal structure reveals a…”
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U2552 methylation at the ribosomal A-site is a negative modulator of translational accuracy by Widerak, Magdalena, Kern, Renée, Malki, Abderrahim, Richarme, Gilbert

“…We have recently identified RrmJ, the first encoded protein of the rrmJ-ftsH heat shock operon, as being the Um 2552 methyltransferase of 23S rRNA, and…”
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Escherichia coli HdeB Is an Acid Stress Chaperone by KERN, Renée, MALKI, Abderrahim, ABDALLAH, Jad, TAGOURTI, Jihen, RICHARME, Gilbert

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YhbO Protects Cells against Multiple Stresses by ABDALLAH, Jad, CALDAS, Teresa, KTHIRI, Fatoum, KERN, Renee, RICHARME, Gilbert

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Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB by Malki, Abderrahim, Le, Hai-Tuong, Milles, Sigrid, Kern, Renée, Caldas, Teresa, Abdallah, Jad, Richarme, Gilbert

“…The acid stress chaperones HdeA and HdeB of Escherichia coli prevent the aggregation of periplasmic proteins at acidic pH. We show in this report that they…”
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The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42 degrees C by Chattopadhyay, Madhab K, Kern, Renée, Mistou, Michel-Yves, Dandekar, Abhaya M, Uratsu, Sandra L, Richarme, Gilbert

“…Since, like other osmolytes, proline can act as a protein stabilizer, we investigated the thermoprotectant properties of proline in vitro and in vivo. In vivo,…”
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Protein Isoaspartate Methyltransferase Is a Multicopy Suppressor of Protein Aggregation in Escherichia coli by KERN, Renée, MALKI, Abderrahim, ABDALLAH, Jad, LIEBART, Jean-Claude, DUBUCS, Catherine, MYEONG HEE YU, RICHARME, Gilbert

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The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase by Kthiri, Fatoum, Le, Hai-Tuong, Tagourti, Jihen, Kern, Renée, Malki, Abderrahim, Caldas, Teresa, Abdallah, Jad, Landoulsi, Ahmed, Richarme, Gilbert

“…Escherichia coli contains two thioredoxins, Trx1 and Trx2, and a thioredoxin-like protein, YbbN, which presents a strong homology in its N-terminal part with…”
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Isolation of a New Hemimethylated DNA Binding Protein Which Regulates dnaA Gene Expression by d'Alençon, Emmanuelle, Taghbalout, Aziz, Bristow, Claire, Kern, Renée, Aflalo, Revital, Kohiyama, Masamichi

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Membrane docking of an aggregation-prone protein improves its solubilization by Tagourti, Jihen, Malki, Abderrahim, Kern, Renée, d'Alençon, Emmanuelle, Richarme, Gilbert

“…We used preS2-S′-β-galactosidase, a three domain fusion protein that aggregates extensively at 43 °C in the cytoplasm of Escherichia coli to search for…”
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Cloning, expression, and purification of the general stress protein YhbO from Escherichia coli by Abdallah, Jad, Kern, Renee, Malki, Abderrahim, Eckey, Viola, Richarme, Gilbert

“…We cloned, expressed, and purified the Escherichia coli yhbO gene product, which is an aminoacid sequence homolog to the Bacillus subtilis general stress…”
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Characterization of the Escherichia coli YedU protein as a molecular chaperone by Malki, Abderrahim, Kern, Renée, Abdallah, Jad, Richarme, Gilbert

“…We have cloned, purified to homogeneity, and characterized as a molecular chaperone the Escherichia coli YedU protein. The purified protein shows a single band…”
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The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase by Caldas, Thérèse, Malki, Abderrahim, Kern, Renée, Abdallah, Jad, Richarme, Gilbert

“…Escherichia coli contains two thioredoxins, Trx1 and Trx2, and a thioredoxin-like protein, YbbN, which presents a strong homology in its N-terminal part with…”
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Replication cycle dependent association of SeqA to the outer membrane fraction of E. coli by d'Alençon, Emmanuelle, Taghbalout, Aziz, Kern, Renée, Kohiyama, Masamichi

“…The hemimethylated oriC binding activity of the E. coli heavy density membrane fraction (outer membrane) was investigated by DNase I footprinting experiments…”
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Co-ordination between membrane oriC sequestration factors and a chromosome partitioning protein, TolC (MukA) by Bahloul, A, Meury, J, Kern, R, Garwood, J, Guha, S, Kohiyama, M

“…oriC DNA in the hemimethylated (but not in the fully methylated) state reacts with an Escherichia coli K-12 outer membrane preparation. This reaction is…”
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Hemi‐methylated oriC DNA binding activity found in non‐specific acid phosphatase by Reshetnyak, Elena, D'Alençon, Emmanuelle, Kern, Renée, Taghbalout, Aziz, Guillaud, Philippe, Kohiyama, Masamichi

“…The lacZ–hobH fusion clone, containing an Escherichia coli DNA segment located at 92 min on the chromosomal map, was screened as a producer of E. coli oriC…”
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Chaperone-like Properties of Lysophospholipids by Kern, Renée, Joseleau-Petit, Danièle, Chattopadhyay, Madhab K., Richarme, Gilbert

“…Lysophospholipids are metabolic intermediates in phospholipid turnover, detergent molecules with membrane-modulating effects, and multifunctional cellular…”
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Competition between the replication initiator DnaA and the sequestration factor SeqA for binding to the hemimethylated chromosomal origin of E. coli in vitro by Taghbalout, Aziz, Landoulsi, Ahmed, Kern, Renée, Yamazoe, Mitsuyoshi, Hiraga, Sota, Holland, Barry, Kohiyama, Masamichi, Malki, Abderrahim

“…Following replication initiation, the replication origin (oriC) in Escherichia coli enters a hemimethylated state at Dam methylation sites which are recognized…”
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