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Published online 27 February 2004

Nucleic Acids Research, 2004, Vol. 32, No. 4 1422-1429
© 2004 Oxford University Press

Conformational change of pseudouridine 55 synthase upon its association with RNA substrate

Kulwadee Phannachet and Raven H. Huang*

Department of Biochemistry, School of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA

*To whom correspondence should be addressed. Tel: +1 217 333 3967; Fax: +1 217 244 5858; Email: huang{at}uiuc.edu

Pseudouridine 55 synthase ({Psi}55S) catalyzes isomerization of uridine (U) to pseudouridine ({Psi}) at position 55 in transfer RNA. The crystal structures of Thermotoga maritima {Psi}55S, and its complex with RNA, have been determined at 2.9 and 3.0 Å resolutions, respectively. Structural comparisons with other families of pseudouridine synthases ({Psi}S) indicate that {Psi}55S may acquire its ability to recognize a stem–loop RNA substrate by two insertions of polypeptides into the {Psi}S core. The structure of apo-{Psi}55S reveals that these two insertions interact with each other. However, association with RNA substrate induces substantial conformational change in one of the insertions, resulting in disruption of interaction between insertions and association of both insertions with the RNA substrate. Specific interactions between two insertions, as well as between the insertions and the RNA substrate, account for the molecular basis of the conformational change.


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