|Journal of Biological Chemistry (2010) 285:28425-33|
|Northeast Structural Genomics Consortium|
(click to unfold)
Bacterial and eukaryotic transfer RNAs have been shown to contain hypermodified adenosine, 2-methylthio-N(6)-threonylcarbamoyladenosine, at position 37 (A(37)) adjacent to the 3'-end of the anticodon, which is essential for efficient and highly accurate protein translation by the ribosome. ...
Using a combination of bioinformatic sequence analysis and in vivo assay coupled to HPLC/MS technique, we have identified, from distinct sequence signatures, two methylthiotransferase (MTTase) subfamilies, designated as MtaB in bacterial cells and e-MtaB in eukaryotic and archaeal cells. Both subfamilies are responsible for the transformation of N(6)-threonylcarbamoyladenosine into 2-methylthio-N(6)-threonylcarbamoyladenosine. Recently, a variant within the human CDKAL1 gene belonging to the e-MtaB subfamily was shown to predispose for type 2 diabetes. CDKAL1 is thus the first eukaryotic MTTase identified so far. Using purified preparations of Bacillus subtilis MtaB (YqeV), a CDKAL1 bacterial homolog, we demonstrate that YqeV/CDKAL1 enzymes, as the previously studied MTTases MiaB and RimO, contain two [4Fe-4S] clusters. This work lays the foundation for elucidating the function of CDKAL1.
|analogs & derivatives metabolism enzymology chemistry genetics |
|Escherichia coli Mice Amino Acid Sequence Adenosine Bacterial Proteins Heat-Shock Proteins Sulfurtransferases Cyclin-Dependent Kinase 5 Escherichia coli Proteins Archaea Sequence Analysis, Protein Bacillus subtilis Humans Molecular Sequence Data RNA, Transfer Threonine Animals |
|50 (Last update: 04/01/2017 11:45:04am)|