Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Bacteria / cytology
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Bacteria / enzymology
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Bacteria / metabolism
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Binding Sites
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Euglena gracilis / cytology
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Euglena gracilis / enzymology
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Euglena gracilis / metabolism
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Methyltransferases / chemistry
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Methyltransferases / metabolism*
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Models, Molecular
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Nucleic Acid Conformation
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RNA, Ribosomal, 16S / chemistry
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RNA, Ribosomal, 16S / metabolism
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Ribosomes / metabolism*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / metabolism
Substances
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RNA, Ribosomal, 16S
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Methyltransferases
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16S rRNA (adenine(1518)-N(6)-adenine(1519)-N(6))-dimethyltransferase