scholarly journals Protein–DNA interactions: structural, thermodynamic and clustering patterns of conserved residues in DNA-binding proteins

2008 ◽  
Vol 36 (18) ◽  
pp. 5922-5932 ◽  
Author(s):  
Shandar Ahmad ◽  
Ozlem Keskin ◽  
Akinori Sarai ◽  
Ruth Nussinov
2020 ◽  
Author(s):  
Mathew Stracy ◽  
Jakob Schweizer ◽  
David J Sherratt ◽  
Achillefs N Kapanidis ◽  
Stephan Uphoff ◽  
...  

ABSTRACTDespite their diverse biochemical characteristics and functions, all DNA-binding proteins share the ability to accurately locate their target sites among the vast excess of non-target DNA. Towards identifying universal mechanisms of the target search, we used single-molecule tracking of 11 diverse DNA-binding proteins in living Escherichia coli. The mobility of these proteins during the target search was dictated by DNA interactions, rather than by their molecular weights. By generating cells devoid of all chromosomal DNA, we discovered that the nucleoid does not pose a physical barrier for protein diffusion, but significantly slows the motion of DNA-binding proteins through frequent short-lived DNA interactions. The representative DNA-binding proteins (irrespective of their size, concentration, or function) spend the majority (58-99%) of their search time bound to DNA and occupy as much as ∼30% of the chromosomal DNA at any time. Chromosome-crowding likely has important implications for the function of all DNA-binding proteins.


Author(s):  
Yanping Zhang ◽  
Pengcheng Chen ◽  
Ya Gao ◽  
Jianwei Ni ◽  
Xiaosheng Wang

Aim and Objective:: Given the rapidly increasing number of molecular biology data available, computational methods of low complexity are necessary to infer protein structure, function, and evolution. Method:: In the work, we proposed a novel mthod, FermatS, which based on the global position information and local position representation from the curve and normalized moments of inertia, respectively, to extract features information of protein sequences. Furthermore, we use the generated features by FermatS method to analyze the similarity/dissimilarity of nine ND5 proteins and establish the prediction model of DNA-binding proteins based on logistic regression with 5-fold crossvalidation. Results:: In the similarity/dissimilarity analysis of nine ND5 proteins, the results are consistent with evolutionary theory. Moreover, this method can effectively predict the DNA-binding proteins in realistic situations. Conclusion:: The findings demonstrate that the proposed method is effective for comparing, recognizing and predicting protein sequences. The main code and datasets can download from https://github.com/GaoYa1122/FermatS.


2020 ◽  
Vol 15 ◽  
Author(s):  
Yi Zou ◽  
Hongjie Wu ◽  
Xiaoyi Guo ◽  
Li Peng ◽  
Yijie Ding ◽  
...  

Background: Detecting DNA-binding proetins (DBPs) based on biological and chemical methods is time consuming and expensive. Objective: In recent years, the rise of computational biology methods based on Machine Learning (ML) has greatly improved the detection efficiency of DBPs. Method: In this study, Multiple Kernel-based Fuzzy SVM Model with Support Vector Data Description (MK-FSVM-SVDD) is proposed to predict DBPs. Firstly, sex features are extracted from protein sequence. Secondly, multiple kernels are constructed via these sequence feature. Than, multiple kernels are integrated by Centered Kernel Alignment-based Multiple Kernel Learning (CKA-MKL). Next, fuzzy membership scores of training samples are calculated with Support Vector Data Description (SVDD). FSVM is trained and employed to detect new DBPs. Results: Our model is test on several benchmark datasets. Compared with other methods, MK-FSVM-SVDD achieves best Matthew's Correlation Coefficient (MCC) on PDB186 (0.7250) and PDB2272 (0.5476). Conclusion: We can conclude that MK-FSVM-SVDD is more suitable than common SVM, as the classifier for DNA-binding proteins identification.


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