Diversity of the Composition of Ribosomal Proteins

Ribosomal proteins with complex and specialized compositions are a critical component of viable cells. The heterogeneity of ribosome composition is indispensably associated with high variability in ribosomal proteins. The professional services related to ribosomal proteomics provided by Creative Biolabs assist scientists and researchers to investigate the diversity of ribosomal proteins within heterogeneous ribosomes.

Over 200 nonhomologous ribosomal proteins have already been identified, only around 30 of which are found in all domains of life. A ribosome of an organism generally presents only 50-80 ribosomal proteins. The globular domains of homologous ribosomal proteins are mostly conserved, whereas the nonglobular extensions present high structural diversity. The conserved core ribosomal proteins contain about 3000 amino acid residues. Except for the core, the variable protein segments contain different amounts of amino acid residues in different domains of life from 1100 to 2700, which suggests the ribosomal proteins are also highly functionally specialized among eukaryotes and prokaryotes.

Structural Variations in Ribosomal Proteins

The apparent functional specializations of ribosomal proteins such as biological activities are reflected in some of the local structural changes in ribosomal proteins. For example, the α-helices in the structure of different ribosomal proteins act as nuclear localization signals or stabilize the interaction between the ribosomal core and rRNA expansions.

An illustration of structural variations in homologous ribosomal proteins of thermophilic bacteria could explain the specialized ribosomal protein of a domain of life adapting to the corresponding environment. Homologous ribosomal protein uS17 is developing an extra thermophile-specific α-helix with the increasing temperature.

Fig. 1 Graphical summary of the functions of mitoribosome-specific ribosomal proteins.¹

Ribosomal Proteins and Diseases

Ribosomal proteins are involved in several ribosomal processes such as DNA repair, apoptosis, and cellular homeostasis in addition to their responsibilities in protein translation. As a result, changes in distinct ribosomal proteins, such as alteration in ribosomal protein function and production, overexpression of ribosomal proteins, and the ribosomal protein encoded gene mutations, can result in a variety of diseases, including neurological diseases, cancers, hematologic diseases, and others.

Variants of the extensions on ribosomal proteins confer targets or resistance to drugs. Those variants also regulate the protein translational rate and accuracy. Comprehensive analysis of ribosomal proteins allows for more accurate identification of ribosomal protein diversity and thus facilitating ribosome-related disease discovery and potential drug development. Creative Biolabs offers a full range of ribosomal proteomics technologies. The rapid and accurate analysis of ribosomal proteins is the best choice for researchers to understand the secondary and tertiary structures and functions of ribosomal proteins.

Our ribosome-related services are available with the following links:

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

Please don’t hesitate to contact us.

Reference

1. Scaltsoyiannes, Vassilis, et al. "Types and functions of mitoribosome-specific ribosomal proteins across eukaryotes." International Journal of Molecular Sciences 23.7 (2022): 3474.