title: tRNA-m1G methyltransferase interactions: touching bases with structure.
abstract: m1G methyltransferase of Escherichia coli is being examined with regard to how specific tRNA substrates are recognized. This enzyme appears to require the entire tRNA structure of optimal activity. Recognition may require specific base contacts as well as phosphate backbone structures embodied in the tRNA structure.
authors.affiliation: Department of Microbiology/Immunology, Virginia Commonwealth University, Medical College of Virginia, Richmond 23298, USA.
authors.forename: W M
authors.initials: WM
authors.lastname: Holmes
authors.forename: C
authors.initials: C
authors.lastname: Andraos-Selim
authors.forename: M
authors.initials: M
authors.lastname: Redlak
mesh_terms: D004926:Escherichia coli / Q000201:enzymology; D006151:Guanosine / Q000031:analogs & derivatives* / Q000378:metabolism; D009690:Nucleic Acid Conformation; D012323:RNA Processing, Post-Transcriptional; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism*; D012354:RNA, Transfer, His / Q000378:metabolism; D012360:RNA, Transfer, Phe / Q000378:metabolism; D012359:tRNA Methyltransferases / Q000378:metabolism*
chemical_list: D012354:RNA, Transfer, His; D012360:RNA, Transfer, Phe; D006151:Guanosine; C020770:1-methylguanosine; D012343:RNA, Transfer; D012359:tRNA Methyltransferases; C036950:tRNA (guanine-N1-)-methyltransferase