Modulation of XPC peptide on binding Tb3+ to Euplotes octocarinatus centrin

Metallomics ◽  
2017 ◽  
Vol 9 (12) ◽  
pp. 1796-1808 ◽  
Author(s):  
Enxian Shi ◽  
Wenlong Zhang ◽  
Yaqin Zhao ◽  
Binsheng Yang
Keyword(s):  
Metal Ions ◽  
Peptide Binding ◽  
Terminal Domain ◽  
Euplotes Octocarinatus

Metal ions weakly enhanced the affinity between EoCen and the XPC peptide, whereas the peptide remarkably modulated the binding of Tb3+ to the N-terminal domain of EoCen. Peptide binding resulted in the dissociation of EoCen aggregates, and the aggregation of EoCen induced by Tb3+ binding was inhibited.

Peptide-Binding Sites As Revealed by the Crystal Structures of the Human Hsp40 Hdj1 C-Terminal Domain in Complex with the Octapeptide from Human Hsp70

Biochemistry ◽  
2010 ◽  
Vol 49 (39) ◽  
pp. 8577-8584 ◽  
Author(s):  
Hironori Suzuki ◽  
Shuji Noguchi ◽  
Hiroshi Arakawa ◽  
Tadaaki Tokida ◽  
Mariko Hashimoto ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Binding Sites ◽  
Peptide Binding ◽  
Terminal Domain ◽  
Human Hsp70

scholarly journals Crystal structure of the trimeric N-terminal domain of ciliate Euplotes octocarinatus centrin binding with calcium ions

2018 ◽  
Vol 27 (6) ◽  
pp. 1102-1108 ◽  
Author(s):  
Wenming Wang ◽  
Yaqin Zhao ◽  
Hongfei Wang ◽  
Bingsheng Yang
Keyword(s):  
Crystal Structure ◽  
Calcium Ions ◽  
Terminal Domain ◽  
Euplotes Octocarinatus

scholarly journals Crosstalk between RNA Pol II C-Terminal Domain Acetylation and Phosphorylation via RPRD Proteins

2018 ◽  
Author(s):  
Ibraheem Ali ◽  
Diego Garrido Ruiz ◽  
Zuyao Ni ◽  
Jeffrey R. Johnson ◽  
Heng Zhang ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Isothermal Calorimetry ◽  
Peptide Binding ◽  
Rna Pol Ii ◽  
Post Translational Modifications ◽  
Pol Ii ◽  
Terminal Domain ◽  
Lysine Residues ◽  
Higher Eukaryotes ◽  
Heptad Repeats

SUMMARYPost-translational modifications of the RNA polymerase II C-terminal domain (CTD) coordinate the transcription cycle. Crosstalk between different modifications is poorly understood. Here, we show how acetylation of lysine residues at position 7 of characteristic heptad repeats (K7ac)—only found in higher eukaryotes—regulates phosphorylation of serines at position 5 (S5p), a conserved mark of polymerases initiating transcription. We identified the regulator of pre-mRNA domain-containing (RPRD) proteins as reader proteins of K7ac. K7ac enhanced CTD peptide binding to the CTD-interacting domain (CID) of RPRD1A and RPRD1B proteins in isothermal calorimetry and molecular modeling experiments. Deacetylase inhibitors increased K7ac- and decreased S5-phosphorylated polymerases, consistent with acetylation-dependent S5 dephosphorylation by an RPRD-associated S5 phosphatase. Consistent with this model, RPRD1B knockdown increased S5p, but enhanced K7ac, indicating RPRD proteins recruit K7 deacetylases, including HDAC1. We also report auto-regulatory crosstalk between K7ac and S5p via RPRD proteins and their interactions with acetyl- and phospho-eraser proteins.

scholarly journals Endonuclease-like activity of the N-terminal domain of Euplotes octocarinatus centrin

RSC Advances ◽  
2017 ◽  
Vol 7 (82) ◽  
pp. 51773-51788 ◽  
Author(s):  
Wenlong Zhang ◽  
Enxian Shi ◽  
Yanan Feng ◽  
Yaqin Zhao ◽  
Binsheng Yang
Keyword(s):  
Nucleotide Excision Repair ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Excision Repair ◽  
Calcium Binding Proteins ◽  
Terminal Domain ◽  
Nucleotide Excision ◽  
Ef Hand ◽  
Euplotes Octocarinatus

Euplotes octocarinatus centrin (EoCen) is a member of the EF-hand superfamily of calcium-binding proteins, which refer to nucleotide excision repair (NER).

scholarly journals Reactivation of Mutant p53 through Interaction of a C-Terminal Peptide with the Core Domain

1999 ◽  
Vol 19 (5) ◽  
pp. 3395-3402 ◽  
Author(s):  
Galina Selivanova ◽  
Ludmila Ryabchenko ◽  
Emmelie Jansson ◽  
Violetta Iotsova ◽  
Klas G. Wiman
Keyword(s):  
Binding Sites ◽  
Peptide Binding ◽  
Human Tumor ◽  
Mutant P53 ◽  
Human Tumor Cells ◽  
Core Domain ◽  
The Core ◽  
Terminal Domain ◽  
P53 Activation ◽  
Growth Suppressor

ABSTRACT A synthetic 22-mer peptide (peptide 46) derived from the p53 C-terminal domain can restore the growth suppressor function of mutant p53 proteins in human tumor cells (G. Selivanova et al., Nat. Med. 3:632–638, 1997). Here we demonstrate that peptide 46 binds mutant p53. Peptide 46 binding sites were found within both the core and C-terminal domains of p53. Lys residues within the peptide were critical for both p53 activation and core domain binding. The sequence-specific DNA binding of isolated tumor-derived mutant p53 core domains was restored by a C-terminal polypeptide. Our results indicate that C-terminal peptide binding to the core domain activates p53 through displacement of the negative regulatory C-terminal domain. Furthermore, stabilization of the core domain structure and/or establishment of novel DNA contacts may contribute to the reactivation of mutant p53. These findings should facilitate the design of p53-reactivating drugs for cancer therapy.

Analysis of Tb3+- and melittin-binding with the C-terminal domain of centrin in Euplotes octocarinatus

2012 ◽  
Vol 132 (4) ◽  
pp. 924-930 ◽  
Author(s):  
Ya-Qin Zhao ◽  
Xiu-Ling Diao ◽  
Jun Yan ◽  
Ya-Nan Feng ◽  
Zhi-Jun Wang ◽  
...  
Keyword(s):  
Terminal Domain ◽  
Euplotes Octocarinatus

Spectral study on the interaction of ciliate Euplotes octocarinatus centrin and metal ions

2007 ◽  
Vol 186 (2-3) ◽  
pp. 178-186 ◽  
Author(s):  
Zhi-Jun Wang ◽  
Ya-Qin Zhao ◽  
Lie-Xiang Ren ◽  
Guo-Ting Li ◽  
Ai-Hua Liang ◽  
...  
Keyword(s):  
Metal Ions ◽  
Spectral Study ◽  
Euplotes Octocarinatus

The interaction between lanthanide (III) and N-terminal domain of Euplotes octocarinatus centrin

2012 ◽  
Vol 87 ◽  
pp. 163-170 ◽  
Author(s):  
Yaqin Zhao ◽  
Jun Yan ◽  
Li Song ◽  
Yanan Feng ◽  
Aihua Liang ◽  
...  
Keyword(s):  
Terminal Domain ◽  
Euplotes Octocarinatus
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