The GndA Microprotein Promotes Cell Growth during Heat Shock in Escherichia coli

Abstract Hundreds of bacterial small open reading frames (sORFs) encoding microproteins of fewer than 50 amino acids have recently been identified. Biological functions have been ascribed to an increasing number of microproteins, some of which play roles in bacterial stress responses. In this work, we provide evidence that GndA, a frameshifted 36-amino acid microprotein encoded in an internal open reading frame overlapping the 6-phosphogluconate dehydrogenase (6PGD) coding sequence (CDS), functions in the response to heat shock. We demonstrate independent contributions of GndA and 6PGD to cell growth at a high temperature. GndA is hydrophobic and associates with the pyruvate dehydrogenase complex and the inner membrane. Consistent with a role in cellular homeostasis, GndA mutations alter the transcriptional response to heat shock. These results demonstrate that GndA promotes bacterial cell growth at high temperatures independently of the 6PGD protein that it overlaps. GndA thus expands the paradigm of bacterial microproteins that function in cellular stress responses.

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Publication Details

Journal
Biochemistry
Published
2026-10-17
DOI
https://doi.org/10.1021/acs.biochem.6c00391
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
0.00

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article

The GndA Microprotein Promotes Cell Growth during Heat Shock in Escherichia coli

Kevin Jiang, Michael G. Mohsen, Sarah A. Slavoff, Farren J. Isaacs et al.
Biochemistry
Bacterial Genetics and Biotechnology
article

The GndA Microprotein Promotes Cell Growth during Heat Shock in Escherichia coli

Kevin Jiang, Michael G. Mohsen, Sarah A. Slavoff, Farren J. Isaacs, Natalia R. Bertolotti, Ane Landajuela, Erdem Karatekin, Christine M. DeRosa, Jessica J. Mohsen, Betel Erkalo, Laura B Quinto, Nikita Dewani, Georgina Dabdoub
article en

Abstract

Abstract Hundreds of bacterial small open reading frames (sORFs) encoding microproteins of fewer than 50 amino acids have recently been identified. Biological functions have been ascribed to an increasing number of microproteins, some of which play roles in bacterial stress responses. In this work, we provide evidence that GndA, a frameshifted 36-amino acid microprotein encoded in an internal open reading frame overlapping the 6-phosphogluconate dehydrogenase (6PGD) coding sequence (CDS), functions in the response to heat shock. We demonstrate independent contributions of GndA and 6PGD to cell growth at a high temperature. GndA is hydrophobic and associates with the pyruvate dehydrogenase complex and the inner membrane. Consistent with a role in cellular homeostasis, GndA mutations alter the transcriptional response to heat shock. These results demonstrate that GndA promotes bacterial cell growth at high temperatures independently of the 6PGD protein that it overlaps. GndA thus expands the paradigm of bacterial microproteins that function in cellular stress responses.

Biochemistry
Centre National de la Recherche Scientifique (FR), Yale University (US)
Howard Hughes Medical Institute, Alfred P. Sloan Foundation, Yale University, Gruber Foundation, Mark Foundation For Cancer Research, Paul G. Allen Frontiers Group, National Institute of General Medical Sciences, National Science Foundation Graduate Research Fellowship Program
Openalex Percentile: Top 15%
Bacterial Genetics and Biotechnology
DOISourceOpenAlex
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