In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein is in vitro (Adpribosyl)ated.
[No authors listed]
摘要
A small protein with high affinity for homologous DNA was isolated from Sulfolobus solfataricus homogenate by mineral acid extraction. It was purified using a two-step procedure including CM-cellulose and RP-HPL chromatographies. The protein was electrophoretically homogeneous, had a molecular weight of 7.147 kDa and an amino acid composition with a high content of lysine and glutamic acid residues. The protein was able to protect DNA against thermal denaturation and DNAse I digestion in a dose-dependent manner. After incubation of the sulfolobal homogenate in the presence of 32P-NAD, followed by the purification steps, the protein was modified by ADPribose, as revealed by reaction product analysis, SDS-PAGE and autoradiography.
KEYWORDS: {{ getKeywords(articleDetailText.words) }}
基因功能
- {{$index+1}}.{{ gene }}
原始数据
| Sample name | Organism | Experiment title | Sample type | Library instrument | Attributes | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| {{attr}} | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| {{ dataList.sampleTitle }} | {{ dataList.organism }} | {{ dataList.expermentTitle }} | {{ dataList.sampleType }} | {{ dataList.libraryInstrument }} | {{ showAttributeName(index,attr,dataList.attributes) }} | |||||||||||||||||||||||||||||||||||||||||||||||||
文献解读
| {{ list.authorName }} {{ list.authorName }} |
