dorsal/arxiv
View SchemaCloning, expression and purification of the general stress protein Yhbo from Escherichia coli
| Authors | Jad Abdallah, Renee Kern, Abderrahim Malki, Viola Eckey, Gilbert Richarme |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0512028 |
| URL | https://arxiv.org/abs/q-bio/0512028 |
| DOI | 10.016/j.pep.2005.11.011 |
| Journal | Protein expression and purification. sous presse (2005) ? |
Abstract
We cloned, expressed and purified the Escherichia coli yhbO gene product, which is homolog to the Bacillus subtilis general stress protein 18 (the yfkM gene product), the Pyrococcus furiosus intracellular protease PfpI, and the human Parkinson disease protein DJ-1. The gene coding for YhbO was generated by amplifying the yhbO gene from E. coli by polymerase chain reaction. It was inserted in the expression plasmid pET-21a, under the transcriptional control of the bacteriophage T7 promoter and lac operator. A BL21(DE3) E. coli strain transformed with the YhbO-expression vector pET-21a-yhbO, accumulates large amounts of a soluble protein of 20 kDa in SDS-PAGE that matches the expected YhbO molecular weight. YhbO was purified to homogeneity by HPLC DEAE ion exchange chromatography and hydroxylapatite chromatography and its identity was confirmed by N-terminal sequencing and mass spectrometry analysis. The native protein exists in monomeric, trimeric and hexameric forms.
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"abstract": "We cloned, expressed and purified the Escherichia coli yhbO gene product,\nwhich is homolog to the Bacillus subtilis general stress protein 18 (the yfkM\ngene product), the Pyrococcus furiosus intracellular protease PfpI, and the\nhuman Parkinson disease protein DJ-1. The gene coding for YhbO was generated by\namplifying the yhbO gene from E. coli by polymerase chain reaction. It was\ninserted in the expression plasmid pET-21a, under the transcriptional control\nof the bacteriophage T7 promoter and lac operator. A BL21(DE3) E. coli strain\ntransformed with the YhbO-expression vector pET-21a-yhbO, accumulates large\namounts of a soluble protein of 20 kDa in SDS-PAGE that matches the expected\nYhbO molecular weight. YhbO was purified to homogeneity by HPLC DEAE ion\nexchange chromatography and hydroxylapatite chromatography and its identity was\nconfirmed by N-terminal sequencing and mass spectrometry analysis. The native\nprotein exists in monomeric, trimeric and hexameric forms.",
"arxiv_id": "q-bio/0512028",
"authors": [
"Jad Abdallah",
"Renee Kern",
"Abderrahim Malki",
"Viola Eckey",
"Gilbert Richarme"
],
"categories": [
"q-bio.GN"
],
"doi": "10.016/j.pep.2005.11.011",
"journal_ref": "Protein expression and purification. sous presse (2005) ?",
"title": "Cloning, expression and purification of the general stress protein Yhbo from Escherichia coli",
"url": "https://arxiv.org/abs/q-bio/0512028"
},
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