scholarly journals DNA Readout Viewer (DRV): visualization of specificity determining patterns of protein-binding DNA segments

2019 ◽  
Vol 36 (7) ◽  
pp. 2286-2287
Author(s):  
Krisztian Adam ◽  
Zoltan Gyorgypal ◽  
Zoltan Hegedus

Abstract Summary The sequence specific recognition of DNA by regulatory proteins typically occurs by establishing hydrogen bonds and non-bonded contacts between chemical sub-structures of nucleotides and amino acids forming the compatible interacting surfaces. The recognition process is also influenced by the physicochemical and conformational character of the target oligonucleotide motif. Although the role of these mechanisms in DNA-protein interactions is well-established, bioinformatical methods rarely address them directly, instead binding specificity is mostly assessed at nucleotide level. DNA Readout Viewer (DRV) aims to provide a novel DNA representation, facilitating in-depth view into these mechanisms by the concurrent visualization of functional groups and a diverse collection of DNA descriptors. By applying its intuitive representation concept for various DNA recognition related visualization tasks, DRV can contribute to unravelling the binding specificity factors of DNA-protein interactions. Availability and implementation DRV is freely available at https://drv.brc.hu. Supplementary information Supplementary data are available at Bioinformatics online.

2020 ◽  
Author(s):  
Adam Soffer ◽  
Morya Ifrach ◽  
Stefan Ilic ◽  
Ariel Afek ◽  
Dan Vilenchik ◽  
...  

AbstractDNA–protein interactions are essential in all aspects of every living cell. Understanding of how features embedded in the DNA sequence affect specific interactions with proteins is challenging but important, since it may contribute to finding the means to regulate metabolic pathways involving DNA–protein interactions. Using a massive experimental benchmark dataset of binding scores for DNA sequences and a machine learning workflow, we describe the binding to DNA of T7 primase, as a model system for specific DNA–protein interactions. Effective binding of T7 primase to its specific DNA recognition se-quences triggers the formation of RNA primers that serve as Okazaki fragment start sites during DNA replication.


1993 ◽  
Vol 229 (3) ◽  
pp. 671-684 ◽  
Author(s):  
Leodevico L. Ilag ◽  
Jean K. Tuech ◽  
Laura A. Beisner ◽  
Roberta A. Sumrada ◽  
Nino L. Incardona

2012 ◽  
Vol 525-526 ◽  
pp. 115-119 ◽  
Author(s):  
Attila Bende ◽  
Ferenc Bogár ◽  
János Ladik

2013 ◽  
Vol 54 ◽  
pp. 79-90 ◽  
Author(s):  
Saba Valadkhan ◽  
Lalith S. Gunawardane

Eukaryotic cells contain small, highly abundant, nuclear-localized non-coding RNAs [snRNAs (small nuclear RNAs)] which play important roles in splicing of introns from primary genomic transcripts. Through a combination of RNA–RNA and RNA–protein interactions, two of the snRNPs, U1 and U2, recognize the splice sites and the branch site of introns. A complex remodelling of RNA–RNA and protein-based interactions follows, resulting in the assembly of catalytically competent spliceosomes, in which the snRNAs and their bound proteins play central roles. This process involves formation of extensive base-pairing interactions between U2 and U6, U6 and the 5′ splice site, and U5 and the exonic sequences immediately adjacent to the 5′ and 3′ splice sites. Thus RNA–RNA interactions involving U2, U5 and U6 help position the reacting groups of the first and second steps of splicing. In addition, U6 is also thought to participate in formation of the spliceosomal active site. Furthermore, emerging evidence suggests additional roles for snRNAs in regulation of various aspects of RNA biogenesis, from transcription to polyadenylation and RNA stability. These snRNP-mediated regulatory roles probably serve to ensure the co-ordination of the different processes involved in biogenesis of RNAs and point to the central importance of snRNAs in eukaryotic gene expression.


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