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

Daniel Klaiman, Michal Amitsur, Shani Blanga-Kanfi, Michal Chai, Darrell R. Davis, Gabriel Kaufmann

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)4704-4714
Number of pages11
JournalNucleic Acids Research
Issue number14
StatePublished - Jul 2007


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