Structural And Functional Characterization of Archaeal Fibrillarin (C/D box protein) in Vivo

Fibrillarin, the methyltransfersase for 2\u27-O-methylation modification in RNAs is the catalytic component of RNP complexes. Most of the information on the role of fibrillarin in Archaea is based on bioinformatics and in vitro data. The essentiality of this protein was not known in Archaea. Similarly, residues important for 2\u27-O-methylation in vivo condition were not known in this domain of life. In this study, we demonstrated that fibrillarin is not essential in Haloferax volcanii. Similarly, we showed that Gm1934 modification of large subunit of rRNA is fibrillarin mediated. Using the crystal structure of Pyrococcus furiosus as a template, we created a homology model of Haloferax volcanii fibrillarin . By combining bioinformatics and biochemical approaches, we identified Hv fibrillarin residues important 2\u27-O-methylation modification in vivo condition