Research focus 研究方向

Recent publications


We showed by circular permutation that a topologically knotted SPOUT RNA methyltransferase, YbeA from E. coli can be unknotted, and fold into a domain-swapped dimer (Ko et al., Structure (2019) 27:1224). Our findings highlight the importance of the universally conserved trefoil-knotted structural motif within the large SPOUT RNA methyltransferase family, which is present in all kingdoms of life. The topological knot likely provides the mechanical strain necessary to bend the cofactor, S-adenosyl-methionine (SAM; AdoMet), to facilitate the methylation reaction.

It is referred by Ya-Ming Hou and co-workers in their commentary.

We have successfully reverse-engineered an unknotted form of a deeply knotted and highly conserved bacterial SPOUT RNA transferase by circular permutation. (Chuang et al., JMB, (2019) 431:857)
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