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Titolo:
Unusual evolutionary history of the tRNA splicing endonuclease EndA: Relationship to the LAGLIDADG and PD-(D/E)XK deoxyribonucleases
Autore:
Bujnicki, JM; Rychlewski, L;
Indirizzi:
Inst Inst Mol & Cell Biol, Bioinformat Lab, PL-02109 Warsaw, Poland Inst Inst Mol & Cell Biol Warsaw Poland PL-02109 PL-02109 Warsaw, Poland
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 3, volume: 10, anno: 2001,
pagine: 656 - 660
SICI:
0961-8368(200103)10:3<656:UEHOTT>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROUP-I INTRON; RESTRICTION-MODIFICATION SYSTEMS; SITE-SPECIFIC ENDONUCLEASE; HOMING ENDONUCLEASE; CRYSTAL-STRUCTURE; DNA RECOGNITION; PI-SCEI; PROTEIN; MOBILE; CLEAVAGE;
Keywords:
protein evolution; endonuclease; homing; intron splicing; restriction-modification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Bujnicki, JM Inst Inst Mol & Cell Biol, Bioinformat Lab, Ul Ks Trojdena 4,PL-02109 Warsaw, Poland Inst Inst Mol & Cell Biol Ul Ks Trojdena 4 WarsawPoland PL-02109
Citazione:
J.M. Bujnicki e L. Rychlewski, "Unusual evolutionary history of the tRNA splicing endonuclease EndA: Relationship to the LAGLIDADG and PD-(D/E)XK deoxyribonucleases", PROTEIN SCI, 10(3), 2001, pp. 656-660

Abstract

The tRNA splicing endoribonuclease EndA from Methanococcus jannaschii is ahomotetramer formed via heterologous interaction between the two pairs of homodimers. Each monomer consists of two alpha/beta domains, the N-terminaldomain (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 tothe PD-(D/E)XK family. Superposition of the NTD on the catalytic domain ofLAGLIDADG homing endonucleases allowed a suggestion to be made about whichamino acid residues of the tRNA splicing nuclease might participate in formation of a presumptive cryptic deoxyribonuclease active site. On the otherhand, the CTD and PD-(D/E)XK endonucleases, represented by restriction enzymes and a phage X exonuclease, were shown to share extensive similarities of the structural framework, to which entirely different active sites mightbe attached in two alternative locations. These findings suggest that EndAevolved from a fusion protein with at least two distinct endonuclease activities: the ribonuclease, which made it an essential "antitoxin" for the cells whose RNA genes were interrupted by introns, and the deoxyribonuclease,which provided the means for homing-like mobility. The residues of the noncatalytic CTDs from the positions corresponding to the catalytic side chains in PD-(D/E)XK deoxyribonucleases map to the surface at the opposite side to the tRNA binding site, for which no function has been implicated. Many restriction enzymes from the PD-(D/E)XK superfamily might have the potentialto maintain an additional active or binding site at the face opposite the deoxyribonuclease active site, a property that can be utilized in protein engineering.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 10:18:02