Interplay between Site-Specific Mutations and Cyclic Nucleotides in Modulating DNA Recognition byEscherichia coliCyclic AMP Receptor Protein†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (28) ◽  
pp. 8901-8910 ◽  
Author(s):  
Jiayin Dai ◽  
Shwu-Hwa Lin ◽  
Carly Kemmis ◽  
Anita J. Chin ◽  
J. Ching Lee
Keyword(s):  
Cyclic Nucleotides ◽  
Dna Recognition ◽  
Receptor Protein ◽  
Site Specific

scholarly journals Distinct Roles for Interfacial Hydration in Site-Specific DNA Recognition by ETS-Family Transcription Factors

2017 ◽  
Vol 121 (13) ◽  
pp. 2748-2758 ◽  
Author(s):  
Suela Xhani ◽  
Shingo Esaki ◽  
Kenneth Huang ◽  
Noa Erlitzki ◽  
Gregory M. K. Poon
Keyword(s):  
Transcription Factors ◽  
Dna Recognition ◽  
Site Specific ◽  
Ets Family

Energetics of Site-Specific DNA Recognition by Integrase Tn916

2005 ◽  
pp. 187-202
Author(s):  
Stoyan Milev ◽  
Hans Rudolf Bosshard ◽  
Ilian Jelesarov
Keyword(s):  
Dna Recognition ◽  
Site Specific

The Bacteriophage P1 Site-specific Recombinase Cin: Recombination Events and DNA Recognition Sequences

1984 ◽  
Vol 49 (0) ◽  
pp. 769-777 ◽  
Author(s):  
S. Iida ◽  
H. Huber ◽  
R. Hiestand-Nauer ◽  
J. Meyer ◽  
T.A. Bickle ◽  
...  
Keyword(s):  
Dna Recognition ◽  
Site Specific ◽  
Bacteriophage P1

Mode of DNA binding with γ-butyrolactone receptor protein CprB from Streptomyces coelicolor revealed by site-specific fluorescence dynamics

2015 ◽  
Vol 1850 (11) ◽  
pp. 2283-2292 ◽  
Author(s):  
Anwesha Biswas ◽  
Satya Narayan ◽  
Mamata V. Kallianpur ◽  
G. Krishnamoorthy ◽  
Ruchi Anand
Keyword(s):  
Dna Binding ◽  
Streptomyces Coelicolor ◽  
Receptor Protein ◽  
Site Specific ◽  
Specific Fluorescence

Linkage of Multiequilibria in DNA Recognition by the D53HEscherichia colicAMP Receptor Protein†

Biochemistry ◽  
2002 ◽  
Vol 41 (50) ◽  
pp. 14935-14943 ◽  
Author(s):  
Shwu-Hwa Lin ◽  
J. Ching. Lee
Keyword(s):  
Dna Recognition ◽  
Receptor Protein

scholarly journals Conservation of genetic information: a code for site-specific DNA recognition.

1993 ◽  
Vol 90 (12) ◽  
pp. 5534-5538 ◽  
Author(s):  
L. F. Harris ◽  
M. R. Sullivan ◽  
D. F. Hickok
Keyword(s):  
Genetic Information ◽  
Dna Recognition ◽  
Site Specific

scholarly journals Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli

1988 ◽  
Vol 253 (3) ◽  
pp. 801-807 ◽  
Author(s):  
A M Gronenborn ◽  
R Sandulache ◽  
S Gärtner ◽  
G M Clore
Keyword(s):  
Escherichia Coli ◽  
Cyclic Amp ◽  
Binding Site ◽  
Cyclic Nucleotides ◽  
Binding Pocket ◽  
Receptor Protein ◽  
Directed Mutagenesis ◽  
Wild Type ◽  
Cyclic Amp Receptor Protein ◽  
Better Than

Mutants in the cyclic AMP binding site of the cyclic AMP receptor protein (CRP) of Escherichia coli have been constructed by oligonucleotide-directed mutagenesis. They have been phenotypically characterized and their ability to enhance the expression of catabolite-repressible operons has been tested. In addition, the binding of cyclic nucleotides to the mutants has been investigated. It is shown that the six mutants made fall into one of three classes: (i) those that bind cyclic AMP better than the wild type protein (Ser-62→Ala) and result in greater transcription enhancement; (ii) those that bind cyclic AMP similarly to wild type (Ser-83→Ala, Ser-83→Lys, Thr-127→Ala, Ser-129→Ala); and (iii) those that do not bind cyclic AMP at all (Arg-82→Leu). Implications of these findings with respect to present models of the cyclic nucleotide binding pocket of CRP are discussed.

Escherichia colicAMP Receptor Protein−DNA Complexes. 1. Energetic Contributions of Half-Sites and Flanking Sequences in DNA Recognition†

Biochemistry ◽  
1998 ◽  
Vol 37 (15) ◽  
pp. 5194-5200 ◽  
Author(s):  
Erica A. Pyles ◽  
Anita J. Chin ◽  
J. Ching Lee
Keyword(s):  
Dna Recognition ◽  
Receptor Protein ◽  
Dna Complexes ◽  
Flanking Sequences

Differentiation Induction In Acute Myeloid Leukemia Using Site-Specific DNA-Targeting

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 3940-3940
Author(s):  
Rahul Palchaudhuri ◽  
Kwan-Keat Ang ◽  
Borja Saez ◽  
David B. Sykes ◽  
Gregory L. Verdine ◽  
...  
Keyword(s):  
Acute Myeloid Leukemia ◽  
Cell Differentiation ◽  
Calcium Binding ◽  
Fusion Proteins ◽  
Myeloid Leukemia ◽  
Dna Recognition ◽  
Control Group ◽  
Site Specific ◽  
Dna Targeting ◽  
Acute Myeloid

Abstract Hoxa9 and Meis1 are overexpressed in >70% of acute myeloid leukemia (AML) and associated with poor prognosis and survival. Hoxa9 and Meis1 interact with DNA and PBX to achieve transcription of differentiation-blocking genes. We tested transcriptional repression at Hoxa9-PBX-Meis1 genomic binding sites to induce differentiation in a model of human AML We designed a DNA-recognition strategy based on the known structure of the Hoxa9-PBX-DNA complex by fusing the DNA binding helices of Hoxa9 and PBX to create concise homeodomain fusion proteins that target the Hoxa9-PBX DNA recognition sequence. To confer transcription-repressing properties to the proteins, we attached a transcriptional repressor (sin3 interacting) domain and ectopically expressed this protein in Hoxa9-Meis1 immortalized murine progenitors. Introduction of this transcription repressor protein significantly enabled cell differentiation versus control (51.2% Mac-1high Gr-1high cells versus 11.3% for control). Multiple gene transcripts indicative of differentiation, such as GCSFR, myeloperoxidase, neutrophil elastase, and the calcium binding protein, S100A8, were also elevated in repressor-expressing cells. Furthermore, direct transcriptional targets of Hoxa9 (e.g. SOX2, CD34, FOXP1, FLT3R, DNAJC10) were down regulated in repressor-expressing cells. Importantly, a mutant repressor lacking the DNA-interacting amino acids did not affect transcription of Hoxa9 targets, demonstrating on-target specificity. Repressor-expressing cells also exhibited lower surface expression of c-Kit and Flt3 receptors and when transplanted into mice resulted in a significant increase in disease latency with a 94 day median latency versus 62 day latency for the control group (p value = 0.002). Our results demonstrate that site-specific DNA-targeting using homeodomain fusion proteins can enable AML cell differentiation and significantly increase disease latency. Disclosures: Scadden: Fate Therapeutics: Consultancy, Equity Ownership.

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