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| Title | Alternative ribosomal protein RpmE2 is produced under zinc limitation in and slows translation and bacterial growth. |
|---|---|
| Journal, issue, pages | mBio, Vol. 17, Issue 7, Page e0113726, Year 2026 |
| Publish date | Jul 8, 2026 |
 Authors | Amy L Forehand / Kinga Malezyna / Keena S Thomas / Ian J Glomski / Cynthia Nau Cornelissen / Ahmad Jomaa / Alison K Criss /  |
| PubMed Abstract | To enhance its pathogenic potential, (Gc) pirates zinc from human metal sequestration proteins using TonB-dependent outer membrane transport systems. However, cytoplasmic mechanisms by which Gc ...To enhance its pathogenic potential, (Gc) pirates zinc from human metal sequestration proteins using TonB-dependent outer membrane transport systems. However, cytoplasmic mechanisms by which Gc adapts to zinc limitation are still uncharacterized. and transcripts, encoding alternative L31 and L36 ribosomal proteins, respectively, which are not predicted to bind zinc, are significantly more abundant in zinc-limited Gc. In other bacterial species, alternative ribosomal proteins replace canonical zinc-binding ribosomal proteins when zinc availability is low, enabling growth under metal limitation. We found that Gc and are in an operon and transcriptionally induced under zinc limitation by derepression via the zinc uptake regulator Zur, while genes encoding canonical proteins and are not zinc-regulated. In contrast to other bacteria, ribosomes in zinc-limited Gc contained both RpmE2 and RpmE. Furthermore, Gc deleted for RpmE2 and RpmJ2 grew better than the wild-type parent under zinc limitation. Gc engineered to produce only RpmE2 exhibited a growth defect relative to RpmE-only Gc, regardless of zinc availability. Moreover, ribosomes from RpmE2-only Gc had reduced translation . Thus, unlike other bacteria, the alternative L31 protein RpmE2 is not functionally equivalent to the canonical RpmE in Gc. Instead, the ribosomes of zinc-limited Gc are heterogeneous, containing either alternative or canonical ribosomal proteins. We propose that L31 ribosomal protein alternation allows Gc to withstand zinc limitation by reducing translation and slowing growth, to prolong its survival when encountering host-imposed nutritional immunity. IMPORTANCE: Zinc acquisition is crucial for growth and infectivity of (Gc). However, research on Gc adaptation to zinc limitation has primarily focused on outer and inner membrane zinc transporters. Here, we implicate ribosomal protein alternation in the Gc response to zinc limitation. Ribosomes containing the non-zinc-binding, alternative ribosomal protein RpmE2 are less translationally active, and RpmE2-producing bacteria grow more slowly. This contrasts with reports from other bacteria, where ribosomal protein alternation facilitates growth in zinc-limited conditions. This work uncovers a new way in which ribosomal protein alternation enables bacterial resistance to nutritional immunity. |
 External links | mBio / PubMed:42312858 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.21 - 3.27 Å |
| Structure data |  EMDB-76891: 70S ribosome containing RpmE2 from Neisseria gonorrhoeae  EMDB-76892: 70S ribosome containing RpmE from Neisseria gonorrhoeae |
| Source |
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Neisseria gonorrhoeae FA 1090 (bacteria)