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Titolo:
Rapid evolution of the DNA-binding site in LAGLIDADG homing endonucleases
Autore:
Lucas, P; Otis, C; Mercier, JP; Turmel, M; Lemieux, C;
Indirizzi:
Univ Laval, Ctr Rech Fonct Struct & Ingn Prot, Quebec City, PQ G1K 7P4, Canada Univ Laval Quebec City PQ Canada G1K 7P4 Quebec City, PQ G1K 7P4, Canada
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 4, volume: 29, anno: 2001,
pagine: 960 - 969
SICI:
0305-1048(20010215)29:4<960:REOTDS>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROUP-I INTRON; RIBOSOMAL-RNA GENE; CHLAMYDOMONAS-REINHARDTII; ENCODED ENDONUCLEASE; CRYSTAL-STRUCTURE; MITOCHONDRIAL-DNA; CEUI ENDONUCLEASE; RECOGNITION SITE; ESCHERICHIA-COLI; CLEAVAGE SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Lemieux, C Univ Laval, Ctr Rech Fonct Struct & Ingn Prot, Pavillon CharlesEugene Marchand, Quebec City, PQ G1K 7P4, Canada Univ Laval Pavillon Charles Eugene Marchand Quebec City PQ Canada G1K 7P4
Citazione:
P. Lucas et al., "Rapid evolution of the DNA-binding site in LAGLIDADG homing endonucleases", NUCL ACID R, 29(4), 2001, pp. 960-969

Abstract

Sequence analysis of chloroplast and mitochondrial large subunit rRNA genes from over 75 green algae disclosed 28 new group I intron-encoded proteinscarrying a single LAGLIDADG motif, These putative homing endonucleases form four subfamilies of homologous enzymes, with the members of each subfamily being encoded by introns sharing the same insertion site, We showed that four divergent endonucleases from the I-Crel subfamily cleave the same DNA substrates, Mapping of the 66 amino acids that are conserved among the members of this subfamily on the 3-dimensional structure of I-Crel bound:to itsrecognition sequence revealed that these residues participate in protein folding, homodimerization, DNA recognition and catalysis. Surprisingly, onlyseven of the 21 I-Crel amino acids interacting with DNA are conserved, suggesting that I-Crel and its homologs use different subsets of residues to recognize the same DNA sequence. Our sequence comparison of all 45 single-LADLIDADG proteins identified so far suggests that these proteins share related structures and that there is a weak:pressure in each subfamily to maintain identical protein-DNA contacts. The high sequence variability we observed in the DNA-binding site of homologous LAGLIDADG endonucleases provides insight into how these proteins evolve new DNA specificity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 01:58:00