ARF-B2: A Protein Complex that Specifically Binds to Part of the Anaerobic Response Element of Maize Adh 1
- 1 July 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 93 (3) , 1094-1101
- https://doi.org/10.1104/pp.93.3.1094
Abstract
Crude whole cell extracts maize (Zea mays L.) suspension cells were examined for DNA binding proteins that specifically interact with a portion of the maize Adh1 promoter that was previously shown to be in contact with a trans-acting factor in vivo. A 17 base pair, double-stranded oligonucleotide probe was constructed that centered around a strong in vivo dimethylsulfate footprint (B2) that coincides with part of the anaerobic response element (ARE). Gel retardation assays were used to characterize a major, specific DNA binding protein activity found in the crude extracts. The activity is present in both aerobic and hypoxically treated cultures and has been designated ARF-B2 (ARE binding factor). ARF-B2 appears to be a multicomponent complex, with a 54 kilodalton subunit termed ARF-B2.alpha. in primary contact with the target DNA.This publication has 18 references indexed in Scilit:
- In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene.Plant Cell, 1990
- DNA sequences required for anaerobic expression of the maize alcohol dehydrogenase 1 geneProceedings of the National Academy of Sciences, 1987
- A single polypeptide possesses the binding and transcription activities of the adenovirus major late transcription factor.Molecular and Cellular Biology, 1986
- Anaerobic treatment of maize roots affects transcription of Adh1 and transcript stability.Molecular and Cellular Biology, 1986
- cDNA cloning and induction of the alcohol dehydrogenase gene ( Adh1 ) of maizeProceedings of the National Academy of Sciences, 1982
- Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresisNucleic Acids Research, 1981
- DNA-dependent transcription of adenovirus genes in a soluble whole-cell extract.Proceedings of the National Academy of Sciences, 1980
- The anaerobic proteins of maizeCell, 1980
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970