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Nucleic Acids Research Advance Access originally published online on June 29, 2007
Nucleic Acids Research 2007 35(14):4704-4714; doi:10.1093/nar/gkm494
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Nucleic Acids Research, 2007, Vol. 35, No. 14 4704-4714
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Parallel dimerization of a PrrC-anticodon nuclease region implicated in tRNALys recognition

Daniel Klaiman1, Michal Amitsur1, Shani Blanga-Kanfi1, Michal Chai1, Darrell R. Davis2 and Gabriel Kaufmann1,*

1Department of Biochemistry, Tel Aviv University, Tel Aviv 69978, Israel and 2Department of Medicinal Chemistry, University of Utah, Salt Lake City, 84112 UT, USA

*To whom correspondence should be addressed. Tel: +1 972 3 642 6213; Fax: +1 972 3 640 6834; Email: gabika{at}tauex.tau.ac.il

Received April 15, 2007. Revised June 3, 2007. Accepted June 6, 2007.

The optional Escherichia coli restriction tRNase PrrC represents a family of potential antiviral devices widespread among bacteria. PrrC comprises a functional C-domain of unknown structure and regulatory ABC/ATPase-like N-domain. The possible involvement of a C-domain sequence in tRNALys recognition was investigated using a matching end-protected 11-meric peptide. This mimic, termed here LARP (Lys-anticodon recognizing peptide) UV-cross-linked tRNALys anticodon stem-loop (ASL) analogs and inhibited their PrrC-catalyzed cleavage. Trimming LARP or introducing in it inactivating PrrC missense mutations impaired these activities. LARP appeared to mimic its matching protein sequence in ability to dimerize in parallel, as inferred from the following results. First, tethering Cys to the amino- or carboxy-end of LARP dramatically enhanced the ASL-cross-linking and PrrC-inhibiting activities under suitable redox conditions. Second, Cys-substitutions in a C-domain region containing the sequence corresponding to LARP elicited specific intersubunit cross-links. The parallel dimerization of PrrC's C-domains and expected head-to-tail dimerization of its N-domains further suggest that the NTPase and tRNALys-binding sites of PrrC arise during distinct assembly stages of its dimer of dimers form.


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