Influence of ribosome chemical properties on protein conformation during translation

Tsukuba, Japan—Proteins are synthesized by ribosomes and subsequently released through a tubular channel known as the ribosome tunnel. Recent studies suggest that some proteins start forming functionally important three-dimensional (3D) structures while still inside the ribosome tunnel. However, the exact mechanism underlying this process remains poorly understood.

To address these issues, researchers at the University of Tsukuba have comprehensively analyzed the 3D structures of ribosome tunnels reported to date. Based on this investigation, they developed a cylindrical model called the ribosome environment mimicking model (REMM), which replicates both the inner diameters and chemical properties of ribosome tunnels—key characteristics of the ribosome. For comparison, they also fabricated a conventional carbon nanotube (CNT) model—a tubular molecule solely made of carbon atoms—which replicates only the inner diameter of the tunnel while disregarding its chemical properties.

The team then used molecular dynamics simulations to examine protein structures within these models. Results revealed that the REMM more accurately reproduced the experimentally observed protein structures within the ribosome tunnel than the CNT. Furthermore, chemical diversity in REMM was identified as a key factor contributing to their superior ability to replicate experimental protein structures. Further refinement of REMM is anticipated to enhance our understanding of protein conformations in living cells.

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This work was supported by grants from Japan Society for the Promotion of Science KAKENHI (Grant Numbers: JP22J20084, JP23K16989, 23H04879, 23H02427 and JP21K06094). In this study, MD simulations were performed using the computational resources of Cygnus/Pegasus provided by the Multidisciplinary Cooperative Research Program at the Center for Computational Sciences, University of Tsukuba (Project codes: LSC, MOLBIO, and BIOSIM).

_{Original Paper}

Title of original paper:
Ribosome Tunnel Environment Drives the Formation of α-helix During Co-Translational Folding

Journal:
Journal of Chemical Information and Modeling

DOI:
10.1021/acs.jcim.4c00901

_{Correspondence}

Associate Professor HARADA, Ryuhei
Center for Computational Sciences, University of Tsukuba

YASUDA, Takunori
JSPS Research Fellowship for Young Scientists DC1 / Doctoral Programs in Biology, Degree Programs in Life and Earth Sciences, Graduate School of Science and Technology, University of Tsukuba

_{Related Link}

Center for Computational Sciences