Proteomics and Non-proteomics Approaches to Study Stable and Transient Protein-Protein Interactions

Abstract

Of the 25,000-30,000 human genes, about 2 % code for proteins. However, there are about 1-2 million protein entities. This is primarily due to alternative splicing, posttranslational modifications (PTMs) or protein-protein interactions. Proteomics sets out to identify proteins, their sequence and known modifications as well as their quantitation in a biological sample for the purpose of understanding biological processes, protein cellular functions, and their physiological and pathological involvement in diseases.Proteins interact at the molecular level with other proteins, nucleic acids, lipids, carbohydrates and metabolites to perform numerous cellular activities. Protein complexes can consist of sets of more stably (stable PPIs) and less stably (transient PPIs) interacting proteins or combination of both. Here, we discuss the proteomics and nonproteomics approaches to study stable and transient PPIs.

Protein-protein interactions in plant antioxidant defense

“…However, it suffers from a high occurrence of false positive and false negative interactions ( Sprinzak et al., 2003 ) and the inability to study membrane proteins. In addition, the heterologous system of yeast limits the studies of the PTM-dependent interactions in plants ( Ngounou Wetie et al., 2019 ) and cannot reveal the indirect interaction of proteins in a multiprotein complex. It has to be noted that the drawbacks of Y2H have been improved by various modifications ( Xing et al., 2016 ).…”