Literature DB >> 33767294

Trivial and nontrivial error sources account for misidentification of protein partners in mutual information approaches.

Camila Pontes1, Miguel Andrade1, José Fiorote1, Werner Treptow2.   

Abstract

The problem of finding the correct set of partners for a given pair of interacting protein families based on multi-sequence alignments (MSAs) has received great attention over the years. Recently, the native contacts of two interacting proteins were shown to store the strongest mutual information (MI) signal to discriminate MSA concatenations with the largest fraction of correct pairings. Although that signal might be of practical relevance in the search for an effective heuristic to solve the problem, the number of MSA concatenations with near-native MI is large, imposing severe limitations. Here, a Genetic Algorithm that explores possible MSA concatenations according to a MI maximization criteria is shown to find degenerate solutions with two error sources, arising from mismatches among (i) similar and (ii) non-similar sequences. If mistakes made among similar sequences are disregarded, type-(i) solutions are found to resolve correct pairings at best true positive (TP) rates of 70%-far above the very same estimates in type-(ii) solutions. A machine learning classification algorithm helps to show further that differences between optimized solutions based on TP rates are not artificial and may have biological meaning associated with the three-dimensional distribution of the MI signal. Type-(i) solutions may therefore correspond to reliable results for predictive purposes, found here to be more likely obtained via MI maximization across protein systems having a minimum critical number of amino acid contacts on their interaction surfaces (N > 200).

Entities:  

Year:  2021        PMID: 33767294     DOI: 10.1038/s41598-021-86455-0

Source DB:  PubMed          Journal:  Sci Rep        ISSN: 2045-2322            Impact factor:   4.379


  5 in total

1.  In silico two-hybrid system for the selection of physically interacting protein pairs.

Authors:  Florencio Pazos; Alfonso Valencia
Journal:  Proteins       Date:  2002-05-01

Review 2.  Specificity in two-component signal transduction pathways.

Authors:  Michael T Laub; Mark Goulian
Journal:  Annu Rev Genet       Date:  2007       Impact factor: 16.830

3.  Inferring interaction partners from protein sequences.

Authors:  Anne-Florence Bitbol; Robert S Dwyer; Lucy J Colwell; Ned S Wingreen
Journal:  Proc Natl Acad Sci U S A       Date:  2016-09-23       Impact factor: 11.205

4.  Coevolutive, evolutive and stochastic information in protein-protein interactions.

Authors:  Miguel Andrade; Camila Pontes; Werner Treptow
Journal:  Comput Struct Biotechnol J       Date:  2019-11-20       Impact factor: 7.271

5.  Accurate prediction of protein-protein interactions from sequence alignments using a Bayesian method.

Authors:  Lukas Burger; Erik van Nimwegen
Journal:  Mol Syst Biol       Date:  2008-02-12       Impact factor: 11.429

  5 in total

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