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Oktawia Korcz, Tomasz Włodarski (Department of Bioinformatics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul. Pawińskiego 5A, 02-106 Warsaw, Poland)
The ribosomal exit tunnel guides the nascent polypeptide chain to exit the ribosome during protein synthesis. It spans the large ribosomal subunit and is shaped by ribosomal RNA, five universal proteins: uL4, uL22, uL23, uL24 and uL29 and one archaea and eukaryotic specific - eL39, which is located near the tunnel’s exit. The exact role of eL39 in co-translational protein folding remains unclear. Interestingly, RPL39L, a paralog of RPL39 found only in mammals and sharing 92% sequence similarity, displays heterogeneous expression across tissues. Experimental studies suggest that its overexpression could reduce protein aggregation, hinting at its potential role in promoting the proper folding of nascent chains.To study eL39 in more detail and understand its role in protein synthesis, we conducted an extensive bioinformatics analysis of its homologs using sequences from UniProt and structural data from PDB and AlphaFoldDB. This bioinformatics study is part of our ongoing effort to characterise ribosomal proteins involved in co-translational protein folding, which will provide novel insights into this process.