期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 15, 期 5, 页码 534-536出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1408
关键词
-
资金
- NIGMS NIH HHS [GM62432, GM066900] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据