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Browsing SOP - Scholarly Publications by Author "Malki, Abderrahim"

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Browsing SOP - Scholarly Publications by Author "Malki, Abderrahim"

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  • Characterization of the Escherichia coli YedU protein as a molecular chaperone 
    Malki, Abderrahim; Kern, Renee; Abdallah, Jad; Richarme, Gilbert (2016-07-19)
    We have cloned, purified to homogeneity, and characterized as a molecular chaperone the Escherichia coli YedU protein. The purified protein shows a single band at 31 kDa on SDS–polyacrylamide gels and forms dimers in ...
  • Cloning, expression, and purification of the general stress protein YhbO from Escherichia coli 
    Abdallah, Jad; Kern, Renee; Malki, Abderrahim; Eckey, Viola; Richarme, Gilbert (2016-07-19)
    We cloned, expressed, and purified the Escherichia coli yhbO gene product, which is an aminoacid sequence homolog to the Bacillus subtilis general stress protein 18 (the yfkM gene product), the Pyrococcus furiosus intracellular ...
  • Escherichia coli HdeB Is an Acid Stress Chaperone 
    Kern, Renee; Malki, Abderrahim; Abdallah, Jad; Tagourti, Jihen; Richarme, Gilbert (2016-07-19)
    We cloned, expressed, and purified the hdeB gene product, which belongs to the hdeAB acid stress operon. We extracted HdeB from bacteria by the osmotic-shock procedure and purified it to homogeneity by ionexchange chromatography ...
  • The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase 
    Caldas, Thérèse; Kern, Renee; Malki, Abderrahim; Abdallah, Jad; Richarme, Gilbert (2016-07-19)
    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 thioredoxin 1 and 2. YbbN, however, does not possess the canonical ...
  • Peptidase Activity of the Escherichia coli Hsp31 Chaperone 
    Malki, Abderrahim; Caldas, Therese; Abdallah, Jad; Kern, Renee; Eckey, Viola; Kim, So Jung; Cha, Sun-Shin; Mori, Hirotada; Richard, Richarme (2016-07-19)
    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 putative Cys184, His185, and Asp213 catalytic triad similar ...
  • Protein Isoaspartate Methyltransferase Is a Multicopy Suppressor of Protein Aggregation in Escherichia coli 
    Kern, Renee; Malki, Abderrahim; Abdallah, Jad; Lebart, Jean-Claude; Dubucs, Catherine; Hee Yu, Myeong; Richarme, Gilbert (2016-07-19)
    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 multicopy suppressors of protein aggregation and inclusion body formation ...
  • Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB 
    Malki, Abderrahim; Le, Hai-Tuong; Milles, Sigrid; Kern, Renee; Caldas, Teresa; Abdallah, Jad; Richarme, Gilbert (2016-07-19)
    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 also form mixed aggregates with proteins that have failed to be ...
  • The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase 
    Kthiri, Fatoum; Le, Hai-Tuong; Tagourti, Jihen; Kern, Renee; Malki, Abderrahim; Caldas, Teresa; Abdallah, Jad; Landoulsi, Ahmed; Richarme, Gilbert (2016-07-19)
    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 thioredoxins, and possesses a 20 kDa C-terminal part of unknown ...

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