ArticleScientific reports2019
Prevention of EloR/KhpA heterodimerization by introduction of site-specific amino acid substitutions renders the essential elongasome protein PBP2b redundant in Streptococcus pneumoniae.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 24 citations in OpenAlex.
- Molecular genetic characterization of bacterial KH-domain proteins.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structures reveal a conserved architecture for raiA noncoding RNA.Nucleic acids research · 2026Article
- Remodeling of RNA-binding proteome and RNA-mediated regulation as a new layer of control of sporulation.mSystems · 2025Article
- KH-R3H domain cooperation in RNA recognition by the global RNA-binding protein KhpB.Nature communications · 2025Article
- NABhClassifier Server: A Tool for the Identification of Helical Nucleic Acid-Binding Sequences in Proteins.Journal of chemical information and modeling · 2025Article
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- A global survey of small RNA interactors identifies KhpA and KhpB as major RNA-binding proteins in Fusobacterium nucleatum.Nucleic acids research · 2024Article
- Negative regulation of MurZ and MurA underlies the essentiality of GpsB- and StkP-mediated protein phosphorylation in Streptococcus pneumoniae D39.Molecular microbiology · 2023Article
- DivIVA Interacts with the Cell Wall Hydrolase MltG To Regulate Peptidoglycan Synthesis in Streptococcus suis.Microbiology spectrum · 2023Article
- Masters of Misdirection: Peptidoglycan Glycosidases in Bacterial Growth.Journal of bacteriology · 2023Review
- Grad-seq analysis ofmicroLife · 2023Article
- KH domain proteins: Another family of bacterial RNA matchmakers?Molecular microbiology · 2022Review
- EloR interacts with the lytic transglycosylase MltG at midcell inJournal of bacteriology · 2021Article
- Grad-seq identifies KhpB as a global RNA-binding protein inmicroLife · 2021Article
- Grad-seq in a Gram-positive bacterium reveals exonucleolytic sRNA activation in competence control.The EMBO journal · 2020Article
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5 authors at 1 institution in 1 country.
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Abstract
The RNA binding proteins EloR and KhpA are important components of the regulatory network that controls and coordinates cell elongation and division in S. pneumoniae. Loss of either protein reduces cell length, and makes the essential elongasome proteins PBP2b and RodA dispensable. It has been shown previously in formaldehyde crosslinking experiments that EloR co-precipitates with KhpA, indicating that they form a complex in vivo. In the present study, we used 3D modeling and site directed mutagenesis in combination with protein crosslinking to further study the relationship between EloR and KhpA. Protein-protein interaction studies demonstrated that KhpA forms homodimers and that KhpA in addition binds to the KH-II domain of EloR. Site directed mutagenesis identified isoleucine 61 (I61) as crucial for KhpA homodimerization. When substituting I61 with phenylalanine, KhpA lost the ability to homodimerize, while it still interacted clearly with EloR. In contrast, both homo- and heterodimerization were lost when I61 was substituted with tyrosine. By expressing these KhpA versions in S. pneumoniae, we were able to show that disruption of EloR/KhpA heterodimerization makes the elongasome redundant in S. pneumoniae. Of note, loss of KhpA homodimerization did not give rise to this phenotype, demonstrating that the EloR/KhpA complex is crucial for regulating the activity of the elongasome. In support of this conclusion, we found that localization of KhpA to the pneumococcal mid-cell region depends on its interaction with EloR. Furthermore, we found that the EloR/KhpA complex co-localizes with FtsZ throughout the cell cycle.
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