Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 5, Pages 534-536Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1408
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Funding
- NIGMS NIH HHS [GM62432, GM066900] Funding Source: Medline
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In contrast to the diversity of most ribosomal RNA modification patterns and systems, the KsgA methyltransferase family seems to be nearly universally conserved along with the modifications it catalyzes. Our data reveal that KsgA interacts with small ribosomal subunits near functional sites, including Initiation factor 3 and 50S subunit binding sites. These findings suggest a checkpoint role for this modification system and offer a functional rationale for the unprecedented level of conservation.
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