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Titolo:
Degeneration of a homing endonuclease and its target sequence in a wild yeast strain
Autore:
Gimble, FS;
Indirizzi:
Texas A&M Univ Syst, Hlth Sci Ctr, Inst Biosci & Technol, Ctr Genome Res, Houston, TX 77030 USA Texas A&M Univ Syst Houston TX USA 77030 enome Res, Houston, TX 77030 USA
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 20, volume: 29, anno: 2001,
pagine: 4215 - 4223
SICI:
0305-1048(20011015)29:20<4215:DOAHEA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROUP-I INTRON; PROTON-TRANSLOCATING ATPASE; SITE-DIRECTED MUTAGENESIS; PI-SCEI ENDONUCLEASE; CRYSTAL-STRUCTURE; DNA-BINDING; SACCHAROMYCES-CEREVISIAE; MUTATIONAL ANALYSIS; AFFINITY CLEAVAGE; RECOGNITION SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Gimble, FS Texas A&M Univ Syst, Hlth Sci Ctr, Inst Biosci & Technol, Ctr Genome Res, 2121 W Holcombe Blvd, Houston, TX 77030 USA Texas A&M Univ Syst 2121 W Holcombe Blvd Houston TX USA 77030 A
Citazione:
F.S. Gimble, "Degeneration of a homing endonuclease and its target sequence in a wild yeast strain", NUCL ACID R, 29(20), 2001, pp. 4215-4223

Abstract

Mobile introns and inteins self-propagate by 'homing', a gene conversion process initiated by site-specific homing endonucleases. The VMA intein, which encodes the PI-Scel endonuclease in Saccharomyces cerevisiae, is presentin several different yeast strains. Surprisingly, a wild wine yeast (DH1-1A) contains not only the intein(+) allele, but also an inteinless allele that has not undergone gene conversion. To elucidate how these two alleles co-exist, we characterized the endonuclease encoded by the DH1-1A intein+ allele and the target site in the intein(-) allele. Sequence analysis revealsseven mutations in the 31 bp recognition sequence, none of which occurs atpositions that are individually critical for activity. However, binding and cleavage of the sequence by PI-Scel is reduced 10-fold compared to the S.cerevisiae target. The PI-Scel analog encoded by the DH1-1A intein+ allele contains 11 mutations at residues in the endonuclease and protein splicing domains. None affects protein splicing, but one, a R417Q substitution, accounts for most of the decrease in DNA cleavage and DNA binding activity of the DH1-1A protein. Loss of activity in the DH1-1A endonuclease and target site provides one explanation for co-existence of the intein(+) and intein- alleles.

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Documento generato il 31/03/20 alle ore 08:45:22