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3. Trascriptional activation by recruitment

Author

Ptashne, Mark and Gann, Alexander

Subjects
Gene expression -- Research, Histones -- Genetic aspects, DNA -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Scientific evidence to support the hypothetical gene activation recruitment mechanism indicates that histones actively block the activation site on the deoxyribonucleic acid molecule from holoenzyme activation. Histone depletion results in increased gene expression while high levels of histone are capable of halting transcription. This research suggests histones play a significant role in gene regulation.

Published
1997

5. An HMG-like protein that can switch a transcriptional activator to a repressor

Author

Lehming, Norbert, Thanos, Dimitris, Brickman, Joshua M., Ma, Jun, Maniatls, Tom, and Ptashne, Mark

Subjects
Genetic transcription -- Regulation, Drosophila -- Observations, Proteins -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

A Drosophila HMGI protein, DSP1, switches the transcriptional activators Dorsal and NF-KB to repressors. The switching mechanism involves a negative regulatory element that is present near the Dorsal-binding areas in the Zen enhancer and near the NF-KB-binding region in the human interferon-beta promoter. The HMG-like proteins help identify if a specific regulator serves as a transcriptional activator or repressor.

Published
1994

6. New eukaryotic transcriptional repressors

Author

Saha, Shamol, Brickman, Joshua M., Lehming, Norbert, and Ptashne, Mark

Subjects
Genetic transcription -- Regulation, Eukaryotic cells -- Genetic aspects, Genetic code -- Identification and classification, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

An Escherichia coli-encoded sequence attached to a DNA-binding fragment of GAL4 converts the latter into a highly basic repressor. A mutant derivative and a synthetic peptide prove as effective, and sometimes superior. Researchers frequently bind the same GAL4 fragment to other E. coli sequences to create activators. The new repressing regions seem to interact with and inhibit activating regions bound nearby on DNA.

Published
1993

7. DNA recognition by GAL4: structure of a protein-DNA complex

Author

Marmorstein, Ronen, Carey, Michael, Ptashne, Mark, and Harrison, Stephen C.

Subjects
Biochemical genetics -- Research, Genetic transcription -- Regulation, Protein binding -- Genetic aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1992

10. Activators and targets

Author

Ptashne, Mark and Gann, Alexander A.F.

Subjects
Proteins -- Physiological aspects, Eukaryotic cells -- Physiological aspects, Genetic transcription -- Regulation, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1990

13. Structure of a phage 434 Cro-DNA complex

Author

Wolberger, Cynthia, Dong, Yicheng, Ptashne, Mark, and Harrison, Stephen C.

Subjects
Bacteriophages -- Research, Protein binding -- Observations, Lysogeny -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1988

14. How eukaryotic transcriptional activators work

Author

Ptashne, Mark

Subjects
Eukaryotic cells -- Research, Protein binding -- Research, Genetic transcription -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1988

15. Negative effect of the transcriptional activator GAL4

Author

Gill, Grace and Ptashne, Mark

Subjects
DNA -- Research, Genetic transcription -- Research, Yeast fungi -- Biotechnology, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1988

16. GAL4 activates transcription in Drosophila

Author

Fischer, Janice A., Giniger, Edward, Maniatis, Tom, and Ptashne, Mark

Subjects
Promoters (Genetics) -- Research, Drosophila -- Genetic aspects, Protein binding -- Research, Genetic transcription -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1988

17. More views on Imanishi-Kari

Author

Ptashne, Mark, Eisen, Herman N., Cairns, John, and Yannoutsos, Nicholas

Subjects
Fraud in science -- Investigations, Immunological research -- Investigations, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1991

19. Yeast activators stimulate plant gene expression

Author

Ma, Jun, Przibilla, Elisabeth, Hu, Jim, Bogorad, Lawrence, and Ptashne, Mark

Subjects
Yeast fungi -- Biotechnology, Plant genetics -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1988

29. Sequence of a represser-binding site in the DNA of bacteriophage λ

Author

Maniatis, Tom, Ptashne, Mark, Barrell, B. G., and Donelson, John

Abstract

The sequence of 33 nucleotides immediately preceding the start point of transcription of an operon in bacteriophage lambda has been determined. This region includes recognition sites for lambda repressor and, probably, for other proteins. The sequence contains interdigitating symmetries.

Published
1974
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30. A new-specificity mutant of 434 repressor that defines an amino acid–base pair contact

Author

Wharton, Robin P. and Ptashne, Mark

Abstract

The represser encoded by bacteriophage 434 binds to its operators by inserting a 'recognition' α-helix into the major groove of the DNA1,2. We have identified an amino acid–base pair contact that determines (in part) the DNA-binding specificity of 434 represser. The identification is based on the properties of a 'new-specificity' mutant, named Represser[Ala 28], which bears the substitution of Ala for Gln at the first residue of its recognition α-helix. Represser[Ala 28] binds with high affinity to a particular doubly mutant operator bearing the same substitution at position 1 in each half-site, but does not bind to either the wild-type operator or to other mutant operators. We describe molecular models of residue 28–base pair 1 interactions that account for the binding specificities of both the mutant and wild-type proteins.

Published
1987
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32. Regulatory functions of the λrepressor reside in the amino-terminal domain

Author

Sauer, Robert T., Pabo, Carl O., Meyer, Barbara J., Ptashne, Mark, and Backman, Keith C.

Abstract

The repressor of bacteriophage λis a protein containing two domains of approximately equal size. Fragments containing the amino-terminal domain of repressor bind specifically to λoperator DNA and mediate positive and negative control of λtranscription both in vitroand in vivo.

Published
1979
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33. Isolation of the 434 Phage Repressor

Author

PIRROTTA, VINCENZO and PTASHNE, MARK

Abstract

The repressor protein of the coliphage 434 has been isolated and its properties compared with those of the λ phage repressor.

Published
1969
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34. GAL4-VP16 is an unusually potent transcriptional activator

Author

Sadowski, Ivan, Ma, Jun, Triezenberg, Steve, and Ptashne, Mark

Subjects
Genetic transcription -- Research, DNA binding proteins -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1988

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