Unusual evolutionary history of the tRNA splicing endonuclease EndA: relationship to the LAGLIDADG and PD-(D/E)XK deoxyribonucleases

Protein Science : a Publication of the Protein Society
Janusz M Bujnicki, L Rychlewski

Abstract

The tRNA splicing endoribonuclease EndA from Methanococcus jannaschii is a homotetramer formed via heterologous interaction between the two pairs of homodimers. Each monomer consists of two alpha/beta domains, the N-terminal domain (NTD) and the C-terminal domain (CTD) containing the RNase A-like active site. Comparison of the EndA coordinates with the publicly available protein structure database revealed the similarity of both domains to site-specific deoxyribonucleases: the NTD to the LAGLIDADG family and the CTD to the PD-(D/E)XK family. Superposition of the NTD on the catalytic domain of LAGLIDADG homing endonucleases allowed a suggestion to be made about which amino acid residues of the tRNA splicing nuclease might participate in formation of a presumptive cryptic deoxyribonuclease active site. On the other hand, the CTD and PD-(D/E)XK endonucleases, represented by restriction enzymes and a phage lambda exonuclease, were shown to share extensive similarities of the structural framework, to which entirely different active sites might be attached in two alternative locations. These findings suggest that EndA evolved from a fusion protein with at least two distinct endonuclease activities: the ribonuclease, which made it an ...Continue Reading

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Citations

May 2, 2006·BMC Genomics·Stanislaw Dunin-HorkawiczJanusz M Bujnicki
Sep 29, 2015·Nature Chemical Biology·Nikolai B SuslovJoseph A Piccirilli
Apr 12, 2017·Nucleic Acids Research·Gaëlle BatotCelia W Goulding
Jan 12, 2013·Journal of Child Neurology·Roberta BattiniFilippo M Santorelli
Jul 23, 2016·The Journal of Biological Chemistry·Parker M JohnsonCelia W Goulding

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