Exploring ribosome composition and newly synthesized proteins through proteomics and potential biomedical applications

Abstract

Introduction: Protein synthesis is the outcome of tightly regulated gene expression which is responsive to a variety of conditions. Efforts are ongoing to monitor individual stages of protein synthesis to ensure maximum efficiency and accuracy. Due to post-transcriptional regulation mechanisms, the correlation between translatome and proteome is higher than between transcriptome and proteome. However, the most accurate approach to assess the key modulators and final protein expression is directly by using proteomics. Areas covered: This review covers various proteomic strategies that were used to better understand post-transcriptional regulation, specifically during and early after translation. The methods that identify both regulatory proteins associated with translational components and newly synthesized proteins are discussed. Expert commentary: Emerging proteomic approaches make it possible to monitor protein dynamics in cells, tissues and whole animals. The ability to detect alteration in protein abundance soon after their synthesis enables earlier recognition of disease causing factors and candidates to prevent/rectify disease phenotype.

Enhancing Comprehensive Analysis of Newly Synthesized Proteins Based on Cleavable Bioorthogonal Tagging

“…The proteome is a dynamic entity, tightly regulated by protein synthesis and degradation to maintain homeostasis in cells. , Change in the cellular proteome can be measured by mass spectrometry (MS) with depth and precision. Measuring changes of newly synthesized proteins (NSPs) over time can substantially improve our understanding of how cells respond to stimuli and maintain homeostasis. , We still need to perform isolation of newly synthesized proteins against the high abundance background proteome under perturbation conditions. , …”

“…3,4 We still need to perform isolation of newly synthesized proteins against the high abundance background proteome under perturbation conditions. 5,6 Considerable efforts have been devoted to the isolation of NSPs in complex biological systems. Dietrich et al 7,8 developed a labeling strategy called BONCAT (bioorthogonal noncanonical amino acid tagging) by labeling mammalian cells with L-azidohomoalanine (AHA), a methionine surrogate with an azide moiety, for NSP enrichment by avidin affinity purification.…”