bims-hypusi Biomed News
on Hypusine and eIF5A
Issue of 2025–02–09
two papers selected by
Sebastian J. Hofer, University of Graz



  1. Plant Sci. 2025 Jan 31. pii: S0168-9452(25)00025-1. [Epub ahead of print]353 112408
      Senescence is a crucial and highly active process in plants, optimising resource allocation and promoting phenotypic plasticity under restricted conditions. It involves global metabolic reprogramming for the organised disintegration and remobilization of resources. Polyamines (PAs) are polycationic biogenic amines prevalent in all eukaryotes and are necessary for cell survival. The commonly used PAs in plants include putrescine, spermidine, and spermine. Notably, the leaf's expression of S-adenosylmethionine decarboxylase and spermidine synthase gene family transcripts significantly changes during senescence. This suggests these genes are critical in spermidine metabolism and may condition metabolic reprogramming. One key role of spermidine in eukaryotes is to provide the 4-aminobutyl group for the posttranslational modification of lysine in eukaryotic translation factor 5A (eIF5A). This modification is catalysed by two sequential enzymatic steps leading to the activation of eIF5A by converting lysine to the unusual amino acid hypusine. Although eIF5A is well characterised to be involved in the translation of proline-rich repeat proteins and other hard-to-read motifs, the biological role of eIF5A has recently been clarified only in mammals. It could be better described at the plant functional level. The expression patterns of eIF5A isoforms and genes encoding machinery responsible for hypusination, differ between induced and developmental leaf senescence. In this paper, we summarise the existing knowledge on spermidine-dependent senescence control mechanisms in plants, raising the possibility that spermidine could be an element of a biological switch controlling the onset of a different type of senescence in an eIF5A-independent and dependent manner.
    Keywords:  Crop; Hypusination; Hypusine; Senescence; Spermidine; eIF5A
    DOI:  https://doi.org/10.1016/j.plantsci.2025.112408
  2. Nat Commun. 2025 Feb 03. 16(1): 1278
      Assembly of functional ribosomal subunits and successfully delivering them to the translating pool is a prerequisite for protein synthesis and cell growth. In S. cerevisiae, the ribosome assembly factor Reh1 binds to pre-60S subunits at a late stage during their cytoplasmic maturation. Previous work shows that the C-terminus of Reh1 inserts into the polypeptide exit tunnel of the pre-60S subunit. Here, we show that Reh1-bound nascent 60S subunits associate with 40S subunits to form actively translating ribosomes. Using selective ribosome profiling, we found that Reh1-bound ribosomes populate open reading frames near start codons. Reh1-bound ribosomes are also strongly enriched for initiator tRNA, indicating they are associated with early elongation. Using cryo-electron microscopy to image Reh1-bound 80S ribosomes, we found they contain A site peptidyl tRNA, P site tRNA and eIF5A, indicating that Reh1 does not dissociate from 60S until translation elongation. We propose that Reh1 is displaced by the elongating peptide chain, making it the last assembly factor released from the nascent 60S subunit during its initial round of translation.
    DOI:  https://doi.org/10.1038/s41467-025-55844-8