Abstract 5

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YlqF are circularly permutated GTPases, as are the related YwaG family of proteins (Leipe, D. et. al. 2002). Recent studies have associated YlqF proteins with ribosomal assembly (Matsuo, Y. et. al. 2006) and the coiled coil domain of YwaG displays close homology with RNAse E (known RNA binding protein) (Anand, B. et. al. 2006). The study was to investigate the function of YlqF proteins. Computational biological methods were applied so as to make inferences on the strucrure, function and evolution of 1pujA (B. subtilis YlqF protein). Structural and functional analyses confirmed the expected GTPase activity of YlqF. Building of a phylogenetic tree displayed the close relationship between YlqF and YawG. Multiple-sequence alignment (MSA) reveiled that YlqF lacks the coiled coil domain of YawG. The current study could not directly indicate YlqF's involvment in ribosomal assembly, however the compiled evidence implies strong conservation of primary and secondary structure between YlqF and YawG. Supportive of the hypothesis that YlqF may be involved in ribosomal assembly.