Protein-induced bending or flexing at the 5'-end of the duck beta A-globin promoter
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články
PubMed
7758968
DOI
10.1016/0378-1119(95)00057-d
PII: 0378-1119(95)00057-D
Knihovny.cz E-zdroje
- MeSH
- DNA vazebné proteiny metabolismus MeSH
- globiny genetika MeSH
- kachny genetika MeSH
- konformace nukleové kyseliny * MeSH
- molekulární sekvence - údaje MeSH
- promotorové oblasti (genetika) genetika MeSH
- sekvence nukleotidů MeSH
- transkripční faktor Sp1 MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- DNA vazebné proteiny MeSH
- globiny MeSH
- transkripční faktor Sp1 MeSH
The 5'-end of the duck beta A-globin promoter contains a protein binding site BS-3/Sp1, the A + T-rich part of which could be involved in DNA bending. Plasmids were constructed using the pBend2 plasmid containing BS-3/Sp1. Circular permutation analysis of the fragments cut out from the plasmids using various restriction endonucleases, in the presence of a partially purified protein extract from embryonic duck erythrocytes, was performed. The results indicate that a rather complicated change in the fragment shape takes place upon protein binding, which is best explained as an induction of two points of bending or flexure within the fragment. Analogical points of flexure may exist at the protein-binding sites of the duck and chicken beta A-globin promoters in spite of differing DNA sequences.
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