The Role of Protein-Protein Interactions in Ribosome

Assembly

Protein-Protein Interactions (PPIs) play a pivotal role in living organisms, participating in and manipulating various aspects of life activities, including cell signaling, immune responses, gene expression regulation, and biosynthesis of biomolecules, in a complex and precise manner. Protein-protein interactions also play a crucial role in the unique and well-known biological process of ribosome assembly. It has been found that protein-ribosomal RNA interaction may be a key element in the binding of certain ribosomal precursors to nascent ribosomes.

Protein-Protein Interactions in Pre-ribosome Assembly

The published ribosome structure exhibits that most ribosomal proteins interact with rRNA. The large number of highly basic arginine and lysine residues in the primary sequences of pre-ribosomal factors means that they may also bind to RNA. Some of the pre-ribosomal proteins are very similar to known ribosomal proteins, which provides a stronger prediction that they will bind to pre-rRNA. Although it can be hypothesized that the sites where these ribosome-like factors bind are later occupied by the corresponding ribosomal proteins, no specific ribosome-like proteins have been described to interact with preRNAs to date. In other respects, the RNA-binding properties of ribosomal pre-proteins can be derived from specific RNA recognition motifs in their sequences. Even though it is not clear what the specific RNA targets of pre-ribosomal proteins are, specific protein-protein interactions between ribosomal precursor factors have been reported. Protein-protein interactions can be divided into three categories: roles that define the subcomplexes of the pre-ribosome, tuned interactions with specific partners, and direct physical interactions that guide the assembly of the pre-ribosome.

Fig. 1 Schematic summary of protein-protein interactions within pre-43S ribosomes.¹

The Key Role of WD Repeat Proteins in Regulating Ribosomal Proteins

It has also been suggested that WD repeat proteins may play a key role by regulating the availability or localization of specific ribosomal proteins in yeast. WD repeat proteins may also affect the localization of ribosomal proteins. It has been found that there is a direct physical interaction between the WD repeat proteins Rrb1 and Rpl3, which may regulate the availability of Rpl3 during ribosome biogenesis in the nucleus. The role of these specific interactions in ribosome assembly is currently being actively investigated. Current studies on the role of pre-ribosomal proteins in the assembly of other ribosomal precursor factors are limited. Some studies have demonstrated that direct interactions between pre-ribosomal proteins can be through direct physical interactions, which are important for the binding of proteins to specific pre-60S complexes.

Overall, protein-protein interactions play a crucial role in the ribosome assembly process, they ensure the correct assembly and functional realization of ribosomes, and also provide important clues to understand ribosome biosynthesis and function, as well as the possible mechanisms by which their aberrant expression in organisms leads to a variety of diseases. Creative Biolabs has established a professional ribosome research platform and has successfully completed several ribosome-related projects. Our services include but are not limited to:

• Ribosome Separation and Extraction Services
• Ribosome Analysis Services
• Ribosomal Marker Antibody Development Services

Feel free to discuss your ribosome related project with our experts. For more details, please feel free to contact us.

Reference

1. Campbell, Melody G., and Katrin Karbstein. "Protein-protein interactions within late pre-40S ribosomes." PloS one 6.1 (2011): e16194.