scholarly journals Identification of Nucleic Acid Binding Sites on Translin-Associated Factor X (TRAX) Protein

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e33035 ◽  
Author(s):  
Gagan Deep Gupta ◽  
Vinay Kumar
2010 ◽  
Vol 429 (2) ◽  
pp. 225-234 ◽  
Author(s):  
Alessa Jaendling ◽  
Ramsay J. McFarlane

Translin, and its binding partner protein TRAX (translin-associated factor-X) are a paralogous pair of conserved proteins, which have been implicated in a broad spectrum of biological activities, including cell growth regulation, mRNA processing, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis, although their precise role in some of these processes remains unclear. Furthermore, translin (with or without TRAX) has nucleic-acid-binding activity and it is apparent that controlling nucleic acid metabolism and distribution are central to the biological role(s) of this protein and its partner TRAX. More recently, translin and TRAX have together been identified as enhancer components of an RNAi (RNA interference) pathway in at least one organism and this might provide critical insight into the biological roles of this enigmatic partnership. In the present review we discuss the biological and the biochemical properties of these proteins that indicate that they play a central and important role in eukaryotic cell biology.


Author(s):  
Zheng Jiang ◽  
Si-Rui Xiao ◽  
Rong Liu

Abstract The biological functions of DNA and RNA generally depend on their interactions with other molecules, such as small ligands, proteins and nucleic acids. However, our knowledge of the nucleic acid binding sites for different interaction partners is very limited, and identification of these critical binding regions is not a trivial work. Herein, we performed a comprehensive comparison between binding and nonbinding sites and among different categories of binding sites in these two nucleic acid classes. From the structural perspective, RNA may interact with ligands through forming binding pockets and contact proteins and nucleic acids using protruding surfaces, while DNA may adopt regions closer to the middle of the chain to make contacts with other molecules. Based on structural information, we established a feature-based ensemble learning classifier to identify the binding sites by fully using the interplay among different machine learning algorithms, feature spaces and sample spaces. Meanwhile, we designed a template-based classifier by exploiting structural conservation. The complementarity between the two classifiers motivated us to build an integrative framework for improving prediction performance. Moreover, we utilized a post-processing procedure based on the random walk algorithm to further correct the integrative predictions. Our unified prediction framework yielded promising results for different binding sites and outperformed existing methods.


2020 ◽  
pp. 217-242
Author(s):  
Dhanusha Yesudhas ◽  
Ambuj Srivastava ◽  
Nisha Muralidharan ◽  
A. Kulandaisamy ◽  
R. Nagarajan ◽  
...  

2018 ◽  
Vol 46 (7) ◽  
pp. 3802-3812 ◽  
Author(s):  
Anshumali Mittal ◽  
Fruzsina Hobor ◽  
Ying Zhang ◽  
Stephen R Martin ◽  
Steven J Gamblin ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Corey H. Yu ◽  
Akash Bhattacharya ◽  
Mirjana Persaud ◽  
Alexander B. Taylor ◽  
Zhonghua Wang ◽  
...  

AbstractSAMHD1 impedes infection of myeloid cells and resting T lymphocytes by retroviruses, and the enzymatic activity of the protein—dephosphorylation of deoxynucleotide triphosphates (dNTPs)—implicates enzymatic dNTP depletion in innate antiviral immunity. Here we show that the allosteric binding sites of the enzyme are plastic and can accommodate oligonucleotides in place of the allosteric activators, GTP and dNTP. SAMHD1 displays a preference for oligonucleotides containing phosphorothioate bonds in the Rp configuration located 3’ to G nucleotides (GpsN), the modification pattern that occurs in a mechanism of antiviral defense in prokaryotes. In the presence of GTP and dNTPs, binding of GpsN-containing oligonucleotides promotes formation of a distinct tetramer with mixed occupancy of the allosteric sites. Mutations that impair formation of the mixed-occupancy complex abolish the antiretroviral activity of SAMHD1, but not its ability to deplete dNTPs. The findings link nucleic acid binding to the antiretroviral activity of SAMHD1, shed light on the immunomodulatory effects of synthetic phosphorothioated oligonucleotides and raise questions about the role of nucleic acid phosphorothioation in human innate immunity.


2003 ◽  
Vol 329 (2) ◽  
pp. 239-251 ◽  
Author(s):  
Piyali Chatterjee ◽  
Kristina L. Brady ◽  
Amanda Solem ◽  
Yugong Ho ◽  
Mark G. Caprara

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