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001-es BibID:	BIBFORM031399
035-os BibID:	(Scopus)0036076817 (WoS)000177036500012 (PMID)12142452
Első szerző:	Fuxreiter Mónika (kutató vegyész)
Cím:	Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases / Monika Fuxreiter, Istvan Simon
Dátum:	2002
ISSN:	0961-8368
Megjegyzések:	Type II restriction endonucleases recognize 4-8 base-pair-long DNA sequences and catalyze their cleavage with remarkable specificity. Crystal structures of the PD-(DE)XK superfamily revealed a common alpha/beta core motif and similar active site. In contrast, these enzymes show little sequence similarity and use different strategies to interact with their substrate DNA. The intriguing question is whether this enzyme family could have evolved from a common origin. In our present work, protein structure stability elements were analyzed and compared in three parts of PD-(DE)XK type II restriction endonucleases: (1) core motif, (2) active-site residues, and (3) residues playing role in DNA recognition. High correlation was found between the active-site residues and those stabilization factors that contribute to preventing structural decay. DNA recognition sites were also observed to participate in stabilization centers. It indicates that recognition motifs and active sites in PD-(DE)XK type II restriction endonucleases should have been evolutionary more conserved than other parts of the structure. Based on this observation it is proposed that PD-(DE)XK type II restriction endonucleases have developed from a common ancestor with divergent evolution.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Protein Science. - 11 : 8 (2002), p. 1978-1983. -
További szerzők:	Simon István
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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