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Protein complexes are composed of two or more associated polypeptide chains that may have different functions. Protein complexes play a critical role for all processes in life and are considered as highly conserved in evolution. In previous studies, protein complexes from E. coli or Mycoplasma pneumoniae have been characterized experimentally, revealing that a typical bacterial cell has on the order of 500 protein complexes. Using gene homology (orthology), these experimentally-observed complexes can be used to predict protein complexes across many species of bacteria. Surprisingly, the majority of protein complexes is not conserved, demonstrating an unexpected evolutionary flexibility.
The current research investigates the evolution of 174 well-characterized (“reference”) protein complexes from E. coli that have three or more subunits. More specifically, we study the evolutionary flexibility by using evidence and patterns of the presence or absence of the subunits across a range of 894 bacterial species and to interpret whether the evolution is due to the loss or gain of a subunit in the protein complex. The purpose of this study is to determine how the presence or absence of a subunit affects the protein complexes’ functionality. We discuss the functional changes observed in a protein complex due to the presence or absence of a particular subunit by using a statistical approach and by confirming its significance.
Bioinformatics | Molecular Biology
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