Peer-reviewedCC BYmicroPublication Biology
Cloning, expression, and purification of small subunit human ribosomal proteins SA/uS2, S2/uS5, S3/uS3, S7/eS7, S8/eS8, S12/eS12, S13/uS15, and S14/uS11 for in vitro characterization.
- 1First-Year Innovation & Research Experience (FIRE), Office of Undergraduate Research, University of Maryland, College Park, MD, USA
Abstract
A recent paper describes an improved method for producing human ribosomal proteins in the soluble fraction of bacterial lysates rather than in inclusion bodies. We have extended this approach to clone, express, and purify additional proteins from the small ribosomal subunit for use in enzymatic and structural assays, as well as protein–protein interaction studies. Here, we show that an N-terminal 6×His-Trx tag enables the soluble expression and purification of human RPS3/uS3, RPS12/eS12, and RPS14/uS11 from E. coli cells. These results expand the repertoire of human ribosomal proteins available for individual characterization outside of the intact ribosomal complex.
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BibTeX
@article{nicholl2026cloning,
title = {{Cloning, expression, and purification of small subunit human ribosomal proteins SA/uS2, S2/uS5, S3/uS3, S7/eS7, S8/eS8, S12/eS12, S13/uS15, and S14/uS11 for in vitro characterization.}},
author = {Shay Nicholl and Madelyn Thompson and Athra Goshtasbi-Gowharrizi and Julia Streit and Jacob Martin and Daniel Outmezguine and Arman Charkhabi and Quira Zeidan},
journal = {microPublication Biology},
year = {2026},
month = jul,
doi = {10.17912/micropub.biology.002010},
url = {https://doi.org/10.17912/micropub.biology.002010},
note = {CC BY},
}
RIS
TY - JOUR
TI - Cloning, expression, and purification of small subunit human ribosomal proteins SA/uS2, S2/uS5, S3/uS3, S7/eS7, S8/eS8, S12/eS12, S13/uS15, and S14/uS11 for in vitro characterization.
AU - Shay Nicholl
AU - Madelyn Thompson
AU - Athra Goshtasbi-Gowharrizi
AU - Julia Streit
AU - Jacob Martin
AU - Daniel Outmezguine
AU - Arman Charkhabi
AU - Quira Zeidan
PY - 2026
DA - 2026/07/01
JO - microPublication Biology
DO - 10.17912/micropub.biology.002010
UR - https://doi.org/10.17912/micropub.biology.002010
AB - A recent paper describes an improved method for producing human ribosomal proteins in the soluble fraction of bacterial lysates rather than in inclusion bodies. We have extended this approach to clone, express, and purify additional proteins from the small ribosomal subunit for use in enzymatic and structural assays, as well as protein–protein interaction studies. Here, we show that an N-terminal 6×His-Trx tag enables the soluble expression and purification of human RPS3/uS3, RPS12/eS12, and RPS14/uS11 from E. coli cells. These results expand the repertoire of human ribosomal proteins available for individual characterization outside of the intact ribosomal complex.
SN - 2578-9430
ER -