Abstract

BackgroundThe small subunit (SSU) processome is a large ribonucleoprotein complex involved in small ribosomal subunit assembly. It consists of the U3 snoRNA and ∼72 proteins. While most of its components have been identified, the protein-protein interactions (PPIs) among them remain largely unknown, and thus the assembly, architecture and function of the SSU processome remains unclear.MethodologyWe queried PPI databases for SSU processome proteins to quantify the degree to which the three genome-wide high-throughput yeast two-hybrid (HT-Y2H) studies, the genome-wide protein fragment complementation assay (PCA) and the literature-curated (LC) datasets cover the SSU processome interactome.ConclusionsWe find that coverage of the SSU processome PPI network is remarkably sparse. Two of the three HT-Y2H studies each account for four and six PPIs between only six of the 72 proteins, while the third study accounts for as little as one PPI and two proteins. The PCA dataset has the highest coverage among the genome-wide studies with 27 PPIs between 25 proteins. The LC dataset was the most extensive, accounting for 34 proteins and 38 PPIs, many of which were validated by independent methods, thereby further increasing their reliability. When the collected data were merged, we found that at least 70% of the predicted PPIs have yet to be determined and 26 proteins (36%) have no known partners. Since the SSU processome is conserved in all Eukaryotes, we also queried HT-Y2H datasets from six additional model organisms, but only four orthologues and three previously known interologous interactions were found. This provides a starting point for further work on SSU processome assembly, and spotlights the need for a more complete genome-wide Y2H analysis.

Highlights

  • Direct, pair-wise, physical protein-protein interactions (PPIs) are the foundation of all biological processes

  • We find that coverage of the small subunit (SSU) processome proteinprotein interactions (PPIs) network is remarkably sparse

  • The protein-fragment complementation assay (PCA) dataset has the highest coverage among the genome-wide studies with 27 PPIs between 25 proteins

Read more

Summary

Introduction

Pair-wise (binary), physical protein-protein interactions (PPIs) are the foundation of all biological processes. Efforts to elucidate the interaction network of all proteins within a cell or organism — termed the interactome — has helped identify the architectural and functional blueprint of cellular processes in various model eukaryotic organisms, such as yeast [1,2,3,4,5], Drosophila [6,7,8,9], C. elegans [10,11,12,13,14], Plasmodium [15], Arabidopsis [16,17], mouse [18] and humans [19,20,21,22]. The small subunit (SSU) processome is a large ribonucleoprotein complex involved in small ribosomal subunit assembly. It consists of the U3 snoRNA and ,72 proteins. While most of its components have been identified, the proteinprotein interactions (PPIs) among them remain largely unknown, and the assembly, architecture and function of the SSU processome remains unclear

Objectives
Methods
Results
Discussion
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call