Published online 21 June 2006
© 2006 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-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.
Article |
PrrC-anticodon nuclease: functional organization of a prototypical bacterial restriction RNase
Department of Biochemistry, Tel Aviv University Ramat Aviv 69978, Israel
*To whom correspondence should be addressed. Tel: 972 3 642 6213; Fax: 972 3 640 6834; Email: gabika{at}tauex.tau.ac.il
Received March 26, 2006. Revised May 22, 2006. Accepted May 25, 2006.
The tRNALys anticodon nuclease PrrC is associated in latent form with the type Ic DNA restriction endonuclease EcoprrI and activated by a phage T4-encoded inhibitor of EcoprrI. The activation also requires the hydrolysis of GTP and presence of dTTP and is inhibited by ATP. The N-proximal NTPase domain of PrrC has been implicated in relaying the activating signal to a C-proximal anticodon nuclease site by interacting with the requisite nucleotide cofactors [Amitsur et al. (2003) Mol. Microbiol., 50, 129–143]. Means described here to bypass PrrC's self-limiting translation and thermal instability allowed purifying an active mutant form of the protein, demonstrating its oligomeric structure and confirming its anticipated interactions with the nucleotide cofactors of the activation reaction. Mutagenesis and chemical rescue data shown implicate the C-proximal Arg320, Glu324 and, possibly, His356 in anticodon nuclease catalysis. This triad exists in all the known PrrC homologs but only some of them feature residues needed for tRNALys recognition by the Escherichia coli prototype. The differential conservation and consistent genetic linkage of the PrrC proteins with EcoprrI homologs portray them as a family of restriction RNases of diverse substrate specificities that are mobilized when an associated DNA restriction nuclease is compromised.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  N. Keppetipola, R. Jain, B. Meineke, M. Diver, and S. Shuman Structure-activity relationships in Kluyveromyces lactis {gamma}-toxin, a eukaryal tRNA anticodon nuclease RNA, June 1, 2009; 15(6): 1036 - 1044. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Keppetipola and S. Shuman Characterization of the 2',3' cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage {lambda} phosphatase Nucleic Acids Res., December 3, 2007; 35(22): 7721 - 7732. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Bailly-Bechet, M. Vergassola, and E. Rocha Causes for the intriguing presence of tRNAs in phages Genome Res., October 1, 2007; 17(10): 1486 - 1495. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Klaiman, M. Amitsur, S. Blanga-Kanfi, M. Chai, D. R. Davis, and G. Kaufmann Parallel dimerization of a PrrC-anticodon nuclease region implicated in tRNALys recognition Nucleic Acids Res., July 9, 2007; 35(14): 4704 - 4714. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Keppetipola, J. Nandakumar, and S. Shuman Reprogramming the tRNA-splicing activity of a bacterial RNA repair enzyme Nucleic Acids Res., June 28, 2007; 35(11): 3624 - 3630. [Abstract] [Full Text] [PDF]
|
|