⊟Summary[edit | edit source]
- pan ID?: SAUPAN004783000
- symbol?: —
- synonym:
- description?: RNA pseudouridine synthase
- RNA pseudouridine synthase
- ribosomal large subunit pseudouridine synthase D
- RluA family pseudouridine synthase
- RNA pseudouridylate synthase
- ribosomal large subunit pseudouridine synthase, RluD subfamily
- ribosomal large subunitpseudouridine synthase D-like protein
- RluA, Pseudouridylate synthase, 23S RNA-specific
- RluA, Pseudouridylate synthases, 23S RNA-specific
- RNA pseudouridylate synthase family protein
- truncated ribosomal large subunit pseudouridine synthase D, RluD subfamily
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 4992994..4993428
- synteny block?: BlockID0037150
- occurrence?: in 100% of 34 strains
rluA : ribosomal large subunit and tRNA pseudouridine synthase A [1]
Although very few post-transcriptional ribosomal RNA modifications are absolutely required for functional protein synthesis, many residues can be modified to enhance the stability, fidelity and rate of reaction. One such modification is the isomerization of uridine in 23S rRNA at position 746 (E. coli numbering; 791 by S. aureus numbering) into pseudouridine by pseudouridine synthase/isomerase A. RluA can also isomerize a second substrate, transfer RNA containing a uridine at position 32, providing structural support and additional hydrogen bonding potential to the anticodon loop.
RluA is a member of the RluA-like family of pseudouridine synthases (ΨS). There are four potential RluA-like ΨS enzymes known (RluA, RluC, RluD and TruC), of which staphylococci contain only three homologues: SAUPAN003179000, SAUPAN003477000, and SAUPAN004783000. All members contain the same XXHRLD consensus active site sequence and act on different RNA substrates to convert uridines into pseudouridines. SAUPAN003477000 can be unambiguously assigned as "rluD" due to its N-terminal, C-terminal and active site homology to E. coli RluD. The remaining staphylococcal RluA-like ΨS enzymes contain an N-terminal S4-like domain that is absent in E. coli RluA. After removing the S4-like domain, SAUPAN004783000 can be unambiguously assigned as "rluA" due to its truncated N-terminal, C-terminal and active site homology to E. coli RluA. Likewise, N-truncated SAUPAN003179000 aligns most closely with E. coli TruC. Based on the precedent that firmicutes contain only five Ψ residues in 23S rRNA, it is highly likely that staphylococci lack RluC enzymatic activity consistent with the functional assignments above. Therefore, 23S rRNA uridines at positions 955, 2504, and 2580 (E. coli numbering; 999, 2531, and 2607 by S. aureus numbering) are likely to remain uridines.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MKFKIPENFNDLSLRDIFQQLKVPKKDLHHLNMSKDITINDKPARLMDKVHTGDDVFVPT
N315 MKFKIPENFNDLSLRDIFQQLKVPKKDLHHLNMSKDITINDKPARLMDKVHTGDDVFVPT
NCTC8325 MKFKIPENFNDLSLRDIFQQLKVPKKDLHHLNMSKDITINDKPARLMDKVHTGDDVFVPT
Newman MKFKIPENFNDLSLRDIFQQLKVPKKDLHHLNMSKDITINDKPARLMDKVHTGDDVFVPT
USA300_FPR3757 MKFKIPENFNDLSLRDIFQQLKVPKKDLHHLNMSKDITINDKPARLMDKVHTGDDVFVPT
************************************************************
COL IDEKSNYVPSYRYAQIKYEDDDMAIVMKPKGVKTHPNDLKESNTLMNHVIYTIDSDYVEP
N315 IDEKSNYVPSYRYAQIKYEDDDMAIVMKPKGVKTHPNDLKESNTLMNHVIYTIDSDYVEP
NCTC8325 IDEKSNYVPSYRYAQIKYEDDDMAIVMKPKGVKTHPNDLKESNTLMNHVIYTIDSDYVEP
Newman IDEKSNYVPSYRYAQIKYEDDDMAIVMKPKGVKTHPNDLKESNTLMNHVIYTIDSDYVEP
USA300_FPR3757 IDEKSNYVPSYRYAQIKYEDDDMAIVMKPKGVKTHPNDLKESNTLMNHVIYTIDSDYVEP
************************************************************
COL IHRLDQETVGLLIVAKNPLMKKILDRMLEDNDITRIYKANVKALLPLKPQTIDMPIGKDK
N315 IHRLDQETVGLLIVAKNPLMKKILDRMLEDNDITRIYKANVKALLPLKPQTIDMPIGKDK
NCTC8325 IHRLDQETVGLLIVAKNPLMKKILDRMLEDNDITRIYKANVKALLPLKPQTIDMPIGKDK
Newman IHRLDQETVGLLIVAKNPLMKKILDRMLEDNDITRIYKANVKALLPLKPQTIDMPIGKDK
USA300_FPR3757 IHRLDQETVGLLIVAKNPLMKKILDRMLEDNDITRIYKANVKALLPLKPQTIDMPIGKDK
************************************************************
COL FHSNKRRVSPTGQRAITHILTSKMIKEAVCQLEIKLDTGRTHQIRVHLAEIGHPVIGDPL
N315 FHSNKRRVSPTGQRAITHILTSKMIKEAVCQLEIKLDTGRTHQIRVHLAEIGHPVIGDPL
NCTC8325 FHSNKRRVSPTGQRAITHILTSKMIKEAVCQLEIKLDTGRTHQIRVHLAEIGHPVIGDPL
Newman FHSNKRRVSPTGQRAITHILTSKMIKEAVCQLEIKLDTGRTHQIRVHLAEIGHPVIGDPL
USA300_FPR3757 FHSNKRRVSPTGQRAITHILTSKMIKEAVCQLEIKLDTGRTHQIRVHLAEIGHPVIGDPL
************************************************************
COL YGDSTLRQLELESYKIEFVHPLTKEVISVSLDD
N315 YGDSTLRQLELESYKIEFVHPLTKEVISVSLDD
NCTC8325 YGDSTLRQLELESYKIEFVHPLTKEVISVSLDD
Newman YGDSTLRQLELESYKIEFVHPLTKEVISVSLDD
USA300_FPR3757 YGDSTLRQLELESYKIEFVHPLTKEVISVSLDD
*********************************
- ↑ James Ofengand
Ribosomal RNA pseudouridines and pseudouridine synthases.
FEBS Lett: 2002, 514(1);17-25
[PubMed:11904174] [WorldCat.org] [DOI] (P p)Tomoko Hamma, Adrian R Ferré-D'Amaré
Pseudouridine synthases.
Chem Biol: 2006, 13(11);1125-35
[PubMed:17113994] [WorldCat.org] [DOI] (P p)Adrián González-López, Daniel S D Larsson, Ravi Kiran Koripella, Brett N Cain, Martin Garcia Chavez, Paul J Hergenrother, Suparna Sanyal, Maria Selmer
Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane.
Sci Rep: 2024, 14(1);14253
[PubMed:38902339] [WorldCat.org] [DOI] (I e)