scholarly journals 06-P045 A G11A mutation N-terminal to the polyalanine tract in HOXD13 causes limb malformations by altering both the stability and the DNA-binding functions of HOXD13

2009 ◽  
Vol 126 ◽  
pp. S133
Author(s):  
Nathalie Brison ◽  
Sebastian Fantini ◽  
Giulia Vaccari ◽  
Philippe Debeer ◽  
Vincenzo Zappavigna ◽  
...  
Keyword(s):  
Dna Binding ◽  
Limb Malformations ◽  
The Stability ◽  
Polyalanine Tract

An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of .lambda. repressor

Biochemistry ◽  
1986 ◽  
Vol 25 (20) ◽  
pp. 5992-5998 ◽  
Author(s):  
R. T. Sauer ◽  
K. Hehir ◽  
R. S. Stearman ◽  
M. A. Weiss ◽  
A. Jeitler-Nilsson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Lambda Repressor ◽  
Terminal Domain ◽  
The Stability

scholarly journals An ATP/ADP-Dependent Molecular Switch Regulates the Stability of p53-DNA Complexes

1999 ◽  
Vol 19 (11) ◽  
pp. 7501-7510 ◽  
Author(s):  
Andrei L. Okorokov ◽  
Jo Milner
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Cellular Response ◽  
Atp Hydrolysis ◽  
P53 Protein ◽  
Molecular Switch ◽  
Dna Complexes ◽  
Switch Mechanism ◽  
The Stability ◽  
First Time

ABSTRACT Interaction with DNA is essential for the tumor suppressor functions of p53. We now show, for the first time, that the interaction of p53 with DNA can be stabilized by small molecules, such as ADP and dADP. Our results also indicate an ATP/ADP molecular switch mechanism which determines the off-on states for p53-DNA binding. This ATP/ADP molecular switch requires dimer-dimer interaction of the p53 tetramer. Dissociation of p53-DNA complexes by ATP is independent of ATP hydrolysis. Low-level ATPase activity is nonetheless associated with ATP-p53 interaction and may serve to regenerate ADP-p53, thus recycling the high-affinity DNA binding form of p53. The ATP/ADP regulatory mechanism applies to two distinct types of p53 interaction with DNA, namely, sequence-specific DNA binding (via the core domain of the p53 protein) and binding to sites of DNA damage (via the C-terminal domain). Further studies indicate that ADP not only stabilizes p53-DNA complexes but also renders the complexes susceptible to dissociation by specific p53 binding proteins. We propose a model in which the DNA binding functions of p53 are regulated by an ATP/ADP molecular switch, and we suggest that this mechanism may function during the cellular response to DNA damage.

scholarly journals Single-stranded DNA-binding protein enhances the stability of CTG triplet repeats in Escherichia coli.

1996 ◽  
Vol 178 (16) ◽  
pp. 5042-5044 ◽  
Author(s):  
W A Rosche ◽  
A Jaworski ◽  
S Kang ◽  
S F Kramer ◽  
J E Larson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Triplet Repeats ◽  
Single Stranded Dna ◽  
The Stability

scholarly journals Asymmetric arginine dimethylation of RelA provides a repressive mark to modulate TNFα/NF-κB response

2016 ◽  
Vol 113 (16) ◽  
pp. 4326-4331 ◽  
Author(s):  
Anja Reintjes ◽  
Julian E. Fuchs ◽  
Leopold Kremser ◽  
Herbert H. Lindner ◽  
Klaus R. Liedl ◽  
...  
Keyword(s):  
Dna Binding ◽  
Stress Responses ◽  
Structural Changes ◽  
Target Genes ◽  
Direct Interaction ◽  
Type I ◽  
Critical Residue ◽  
The Stability ◽  
Dynamics Simulations ◽  
Protein Arginine Methyltransferase 1

Nuclear factor kappa B (NF-κB) is an inducible transcription factor that plays critical roles in immune and stress responses and is often implicated in pathologies, including chronic inflammation and cancer. Although much has been learned about NF-κB–activating pathways, the specific repression of NF-κB is far less well understood. Here we identified the type I protein arginine methyltransferase 1 (PRMT1) as a restrictive factor controlling TNFα-induced activation of NF-κB. PRMT1 forms a cellular complex with NF-κB through direct interaction with the Rel homology domain of RelA. We demonstrate that PRMT1 methylates RelA at evolutionary conserved R30, located in the DNA-binding L1 loop, which is a critical residue required for DNA binding. Asymmetric R30 dimethylation inhibits the binding of RelA to DNA and represses NF-κB target genes in response to TNFα. Molecular dynamics simulations of the DNA-bound RelA:p50 predicted structural changes in RelA caused by R30 methylation or a mutation that interferes with the stability of the DNA–NF-κB complex. Our findings provide evidence for the asymmetric arginine dimethylation of RelA and unveil a unique mechanism controlling TNFα/NF-κB signaling.

The DNA Binding Protein H-NS Binds to and Alters the Stability of RNA in vitro and in vivo

2004 ◽  
Vol 339 (3) ◽  
pp. 505-514 ◽  
Author(s):  
Cristin C Brescia ◽  
Meenakshi K Kaw ◽  
Darren D Sledjeski
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
The Stability

SIVA1 Regulates the Stability of Single-Stranded DNA-Binding Protein 3 Isoforms

2018 ◽  
Vol 52 (5) ◽  
pp. 707-714
Author(s):  
Z. Yin ◽  
K. Zhang ◽  
X. Peng ◽  
Z. Jiang ◽  
W. Yuan ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
The Stability
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