RNA:(guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited--bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure.
RNA:(guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited--bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure.
复制标题
DOI：
10.1186/1471-2105-3-10
复制
发表时间：
2002-04-03
影响因子：
3
通讯作者：
Rychlewski L
中科院分区：
文献类型：
--
作者：
Bujnicki JM;Rychlewski L
大肠杆菌鸟氨酸-N_2(M2G)甲基转移酶(MTase)RsmC和RsmD修饰16S rRNA的核苷G1207和G966。它们在C末端有一个共同的MTase结构域，在N末端有一个可变区。它们的C-末端结构域与假想的MTase YbiN家族相关，但对N-末端结构域的结构或功能知之甚少。结合使用序列数据库搜索和折叠识别方法，已经证明RsmC和RsmD的N-末端彼此相关，并且它们代表C-末端MTase结构域的“退化”版本。从古生界和真核生物中鉴定出YbiN家族的新成员。推测YbiN以及RsmC和RsmD的两个结构域与革兰氏阳性细菌和古生菌的一个可能的MTase家族密切相关，以来自M.jannaschii的Mj0882蛋白为代表(PDB中为1Dus)。根据序列分析和结构预测的结果，确定了参与辅因子结合、靶标识别和催化的残基，并提出了鸟嘌呤-N_2甲基转移反应的机理。利用已知的Mj0882结构，对真正的和推测的m2G MTase家族的序列-结构-功能关系进行了全面的分析。这些结果为m2G甲基化的机制提供了新的见解，并将作为大量未表征的N-MTase的实验分析的平台。
Escherichia coli guanine-N2 (m2G) methyltransferases (MTases) RsmC and RsmD modify nucleosides G1207 and G966 of 16S rRNA. They possess a common MTase domain in the C-terminus and a variable region in the N-terminus. Their C-terminal domain is related to the YbiN family of hypothetical MTases, but nothing is known about the structure or function of the N-terminal domain. Using a combination of sequence database searches and fold recognition methods it has been demonstrated that the N-termini of RsmC and RsmD are related to each other and that they represent a "degenerated" version of the C-terminal MTase domain. Novel members of the YbiN family from Archaea and Eukaryota were also indentified. It is inferred that YbiN and both domains of RsmC and RsmD are closely related to a family of putative MTases from Gram-positive bacteria and Archaea, typified by the Mj0882 protein from M. jannaschii (1dus in PDB). Based on the results of sequence analysis and structure prediction, the residues involved in cofactor binding, target recognition and catalysis were identified, and the mechanism of the guanine-N2 methyltransfer reaction was proposed. Using the known Mj0882 structure, a comprehensive analysis of sequence-structure-function relationships in the family of genuine and putative m2G MTases was performed. The results provide novel insight into the mechanism of m2G methylation and will serve as a platform for experimental analysis of numerous uncharacterized N-MTases.
登录
查看更多内容
影响因子：
3
作者：
Bujnicki JM;Feder M;Radlinska M;Rychlewski L
通讯作者：
Rychlewski L
影响因子：
5.6
作者：
Aravind, L;Koonin, EV
通讯作者：
Koonin, EV
DOI：
10.1038/84104
发表时间：
2001-02-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Goedecke, K;Pignot, M;Weinhold, E
通讯作者：
Weinhold, E
影响因子：
5.8
作者：
Cuff, JA;Clamp, ME;Barton, GJ
通讯作者：
Barton, GJ
DOI：
10.1073/pnas.090102597
发表时间：
2000-05-09
影响因子：
11.1
作者：
Anderson, J;Phan, L;Hinnebusch, AG
通讯作者：
Hinnebusch, AG