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Nucleic Acids Research, 2001, Vol. 29, No. 18 3848-3856
© 2001 Oxford University Press

Bacterial ribonuclease P holoenzyme crosslinking analysis reveals protein interaction sites on the RNA subunit

Stephen M. Sharkady and James M. Nolan*

Department of Biochemistry-SL43, Tulane University Health Sciences Center, 1430 Tulane Avenue, New Orleans, LA 70112-2699, USA

The structure of the Escherichia coli ribonuclease P (RNase P) holoenzyme was investigated by site-directed attachment of an aryl azide crosslink reagent to specific sites in the protein subunit of the enzyme. The sites of crosslinking to the RNase P RNA subunit were mapped by primer extension to several conserved residues and structural features throughout the RNA. The results suggest rearrangement of current tertiary models of the RNA subunit, particularly in regions poorly constrained by earlier data. Crosslinks to the substrate precursor-tRNA were also detected, consistent with previous crosslinking results in the Bacillus subtilis RNase P holoenzyme.

* To whom correspondence should be addressed. Tel: +1 504 584 2453; Fax: +1 504 584 2739; Email: jnolan{at}tulane.edu


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