Document Type

Article

Publication Date

2-5-2021

Identifier

DOI: 10.1038/s41467-021-21053-2; PMCID: PMC7864902

Abstract

The structure of proline prevents it from adopting an optimal position for rapid protein synthesis. Poly-proline-tract (PPT) associated ribosomal stalling is resolved by highly conserved eIF5A, the only protein to contain the amino acid hypusine. We show that de novo heterozygous EIF5A variants cause a disorder characterized by variable combinations of developmental delay, microcephaly, micrognathia and dysmorphism. Yeast growth assays, polysome profiling, total/hypusinated eIF5A levels and PPT-reporters studies reveal that the variants impair eIF5A function, reduce eIF5A-ribosome interactions and impair the synthesis of PPT-containing proteins. Supplementation with 1 mM spermidine partially corrects the yeast growth defects, improves the polysome profiles and restores expression of PPT reporters. In zebrafish, knockdown eif5a partly recapitulates the human phenotype that can be rescued with 1 µM spermidine supplementation. In summary, we uncover the role of eIF5A in human development and disease, demonstrate the mechanistic complexity of EIF5A-related disorder and raise possibilities for its treatment.

Journal Title

Nat Commun

Volume

12

Issue

1

First Page

833

Last Page

833

MeSH Keywords

Adolescent; Amino Acid Sequence; Animals; Child; Developmental Disabilities; Embryo, Nonmammalian; Female; Gene Expression Regulation, Developmental; Humans; Lysine; Male; Microcephaly; Micrognathism; Peptide Initiation Factors; Peptides; Protein Biosynthesis; Protein Conformation; Protein Isoforms; RNA-Binding Proteins; Ribosomes; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Spermidine; Zebrafish; Zebrafish Proteins

Keywords

Amino Acid Sequence; Developmental Disabilities; Embryo, Nonmammalian; Female; Gene Expression Regulation, Developmental; Humans; Lysine; Male; Microcephaly; Micrognathism; Peptide Initiation Factors; Peptides; Protein Biosynthesis; Protein Conformation; Protein Isoforms; RNA-Binding Proteins; Ribosomes; Saccharomyces cerevisiae Proteins; Sequence Alignment; Spermidine; Zebrafish Proteins

Comments

Grant support

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

Publisher's Link: https://www.nature.com/articles/s41467-021-21053-2

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