A conserved rRNA methyltransferase regulates ribosome biogenesis.
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.
Xu
Zhili
Z
Department of Biology, Hutchison Hall 301, University of Rochester, Rochester, New York 14627, USA.
O'Farrell
Heather C
HC
Rife
Jason P
JP
Culver
Gloria M
GM
D000818:Animals; D001419:Bacteria / Q000166:cytology / Q000201:enzymology / Q000378:metabolism; D001665:Binding Sites; D005056:Euglena gracilis / Q000166:cytology / Q000201:enzymology / Q000378:metabolism; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000201:enzymology / Q000378:metabolism
D012336:RNA, Ribosomal, 16S; D008780:Methyltransferases; C047346:16S rRNA (adenine(1518)-N(6)-adenine(1519)-N(6))-dimethyltransferase