Domains of Mnt Repressor: Roles in Tetramer Formation, Protein Stability, and Operator DNA Binding

Biochemistry ◽  
1995 ◽  
Vol 34 (40) ◽  
pp. 13109-13116 ◽  
Author(s):  
Carey D. Waldburger ◽  
Robert T. Sauer
Keyword(s):  
Dna Binding ◽  
Protein Stability ◽  
Tetramer Formation ◽  
Operator Dna ◽  
Mnt Repressor

scholarly journals Influence of supercoiling and sequence context on operator DNA binding with lac repressor.

1987 ◽  
Vol 262 (30) ◽  
pp. 14592-14599 ◽  
Author(s):  
P A Whitson ◽  
W T Hsieh ◽  
R D Wells ◽  
K S Matthews
Keyword(s):  
Dna Binding ◽  
Lac Repressor ◽  
Sequence Context ◽  
Operator Dna

scholarly journals Biochemical characterization of L1 repressor mutants with altered operator DNA binding activity

Bacteriophage ◽  
2012 ◽  
Vol 2 (2) ◽  
pp. 79-88 ◽  
Author(s):  
Amitava Bandhu ◽  
Tridib Ganguly ◽  
Biswanath Jana ◽  
Amritangshu Chakravarty ◽  
Anindya Biswas ◽  
...  
Keyword(s):  
Dna Binding ◽  
Biochemical Characterization ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Operator Dna

scholarly journals Rett syndrome mutation MeCP2 T158A disrupts DNA binding, protein stability and ERP responses

2011 ◽  
Vol 15 (2) ◽  
pp. 274-283 ◽  
Author(s):  
Darren Goffin ◽  
Megan Allen ◽  
Le Zhang ◽  
Maria Amorim ◽  
I-Ting Judy Wang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Protein Stability ◽  
Rett Syndrome ◽  
Binding Protein ◽  
Dna Binding Protein

scholarly journals Autoregulation of DNA Binding and Protein Stability of Kaposi's Sarcoma-Associated Herpesvirus ORF50 Protein

2004 ◽  
Vol 78 (19) ◽  
pp. 10657-10673 ◽  
Author(s):  
Pey-Jium Chang ◽  
George Miller
Keyword(s):  
Dna Binding ◽  
Protein Stability ◽  
Electrophoretic Mobility ◽  
Kaposi's Sarcoma ◽  
Regulatory Region ◽  
Kaposi’S Sarcoma ◽  
Lytic Cycle ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Promoter Dna ◽  
Kaposi’S Sarcoma Associated Herpesvirus

ABSTRACT A transcriptional activator encoded in open reading frame 50 (ORF50) of Kaposi's sarcoma-associated herpesvirus (KSHV) initiates the viral lytic cycle. ORF50 protein activates downstream KSHV target genes by at least two mechanisms: direct recognition of response elements in promoter DNA and interaction with cellular proteins bound to promoter DNA. We have identified a multifunctional regulatory region, present in amino acids (aa) 520 to 535 of ORF50 protein, that controls DNA binding and protein stability. Deletion of aa 521 to 534 or mutation of a basic motif (KKRK) in this regulatory region dramatically enhances DNA binding by ORF50 protein, as shown by electrophoretic mobility shift, DNA affinity chromatography, and chromatin immunoprecipitation assays. Deletion of the regulatory region and mutations in the KKRK motif also lead to abundant expression of an electrophoretic mobility variant, ORF50B, which appears to be a form of ORF50 protein that is decreased in posttranslational modification. Enhanced DNA binding and enhanced expression of ORF50B are independent phenomena. The regulatory region likely inhibits DNA binding through interactions with the DNA binding domain in aa 1 to 390 and destabilizes ORF50B through interactions with a domain located in aa 590 to 650. Mutants in the KKRK motif that are enhanced in DNA binding are nonetheless impaired in activating direct targets, such as polyadenylated nuclear RNA, and indirect targets, such as ORF50 itself. The identification of an autoregulatory region emphasizes that the many functions of ORF50 protein must be subject to exquisite control to achieve optimal KSHV lytic-cycle gene expression.

Cooperative and Anticooperative Effects in Binding of the First and Second Plasmid OsymOperators to a LacI Tetramer: Evidence for Contributions of Non-operator DNA Binding by Wrapping and Looping

1996 ◽  
Vol 260 (5) ◽  
pp. 697-717 ◽  
Author(s):  
Mark M. Levandoski ◽  
Oleg V. Tsodikov ◽  
Diane E. Frank ◽  
Sonya E. Melcher ◽  
Ruth M. Saecker ◽  
...  
Keyword(s):  
Dna Binding ◽  
Operator Dna

Structural insights into conformational switching in the copper metalloregulator CsoR fromStreptomyces lividans

2015 ◽  
Vol 71 (9) ◽  
pp. 1872-1878 ◽  
Author(s):  
Tatiana V. Porto ◽  
Michael A. Hough ◽  
Jonathan A. R. Worrall
Keyword(s):  
Dna Binding ◽  
Bound States ◽  
Transcriptional Response ◽  
Bound State ◽  
Copper Stress ◽  
Side Chain ◽  
Conformational Switching ◽  
X Ray ◽  
Operator Dna ◽  
Structural Insights

Copper-sensitive operon repressors (CsoRs) act to sense cuprous ions and bind them with a high affinity under copper stress in many bacteria. The binding of copper(I) leads to a conformational change in their homotetramer structure, causing disassembly of the operator DNA–CsoR complex and evoking a transcriptional response. Atomic-level structural insight into the conformational switching mechanism between the apo and metal-bound states is lacking. Here, a new X-ray crystal structure of the CsoR fromStreptomyces lividansis reported and compared with a previously reportedS. lividansCsoR X-ray structure crystallized under different conditions. Based on evidence from this new X-ray structure, it is revealed that the conformational switching between states centres on a concertina effect at the C-terminal end of each α2 helix in the homotetramer. This drives the Cys104 side chain, a copper(I)-ligating residue, into a position enabling copper(I) coordination and as a result disrupts the α2-helix geometry, leading to a compacting and twisting of the homotetramer structure. Strikingly, the conformational switching induces a redistribution of electrostatic surface potential on the tetrameric DNA-binding face, which in the copper(I)-bound state would no longer favour interaction with the mode of operator DNA binding.

Recovery of operator DNA binding activity from denatured lactose repressor

Biochemistry ◽  
1976 ◽  
Vol 15 (20) ◽  
pp. 4353-4356 ◽  
Author(s):  
John R. Sadler ◽  
Marianne Tecklenburg
Keyword(s):  
Dna Binding ◽  
Binding Activity ◽  
Lactose Repressor ◽  
Dna Binding Activity ◽  
Operator Dna
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