Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.
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rpsD (PA4239) identified in the PAO1 genome, which encodes a large complement of genes reflecting its environmental adaptability.
"the sequence provides insights into the basis of the versatility and intrinsic drug resistance of P. aeruginosa"
Modulation of decoding fidelity by ribosomal proteins S4 and S5.
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S4 and S5 mutations alter translational accuracy; the S4-S5 interface controls decoding fidelity via open/closed 30S conformations.
"Ribosomal proteins S4 and S5 participate in the decoding and assembly processes on the ribosome and the interaction with specific antibiotic inhibitors of translation"
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Mutations disrupting the S4-S5 interface cause ribosomal ambiguity (ram) phenotypes with increased miscoding.
"the tRNA selection pathway involves a transition between the closed and open conformations of the 30S ribosomal subunit and requires disruption of the interface between the S4 and S5 proteins"
The C-terminus of ribosomal protein uS4 contributes to small ribosomal subunit biogenesis and the fidelity of translation.
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uS4 C-terminal truncations cause both assembly defects and increased miscoding, but assembly requirements are less stringent than decoding requirements.
"the C-terminal requirements for ribosome assembly are less rigid than for mRNA decoding"
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uS4 has additional roles as a translational repressor and in transcription antitermination.
"uS4 is also a translational repressor ... and is involved in transcription antitermination activities"
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uS4 is a primary binding protein that binds 16S rRNA directly to initiate 30S assembly.
"ribosomal protein uS4 helps initiate the assembly of the small subunit by binding directly to 16S rRNA"
Temperature-dependent RNP conformational rearrangements: analysis of binary complexes of primary binding proteins with 16 S rRNA.
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S4-16S rRNA complex undergoes temperature-dependent conformational rearrangements that are prerequisite for downstream 30S assembly.
"Additionally, a temperature-dependent conformational rearrangement was reported for a complex of primary r-protein S4 and 16 S rRNA"
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Conformational changes in 16S rRNA induced by primary binding proteins are consistent with sequential ribosome assembly.
"Some of the architectures achieved in these rearrangements are consistent with subsequent downstream assembly events such as assembly of the secondary and tertiary binding r-proteins"
BioReason-Pro SFT functional summary for rpsD