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  PspGI a type II restriction endonuclease from the extreme thermophile Pyrococcus sp.: Structural and functional studies to investigate an evolutionary relationship with several mesophilic restriction enzymes

Pingoud, V., Conzelmann, C., Kinzebach, S., Sudina, A., Metelev, V., Kubareva, E., et al. (2003). PspGI a type II restriction endonuclease from the extreme thermophile Pyrococcus sp.: Structural and functional studies to investigate an evolutionary relationship with several mesophilic restriction enzymes. Journal of Molecular Biology, 329(5), 913-929. doi:10.1016/S0022-2836(03)00523-0.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8A25-D Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8A26-B
Genre: Zeitschriftenartikel
Alternativer Titel : J. Mol. Biol.

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 Urheber:
Pingoud, Vera, Autor
Conzelmann, Charlotte, Autor
Kinzebach, Steffen, Autor
Sudina, Anna, Autor
Metelev, Valerie, Autor
Kubareva, Elena, Autor
Bujnicki, Janusz M., Autor
Lurz, Rudi1, Autor
Lüder, Gerhild1, Autor
Xu, Shuang-Yong, Autor
Pingoud, Alfred, Autor
Affiliations:
1Max Planck Society, ou_persistent13              

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Schlagwörter: restriction-modification systems; DNA binding; DNA cleavage; cross-linking; electron microscopy
 Zusammenfassung: We present here the first detailed biochemical analysis of an archaeal restriction enzyme. PspGI shows sequence similarity to SsoII, EcoRII, NgoMIV and Cfr10I, which recognize related DNA sequences. We demonstrate here that PspGI, like SsoII and unlike EcoRII or NgoMIV and Cfr10I, interacts with and cleaves DNA as a homodimer and is not stimulated by simultaneous binding to two recognition sites. PspGI and SsoII differ in their basic biochemical properties, viz. stability against chemical denaturation and proteolytic digestion, DNA binding and the pH, MgCl2 and salt-dependence of their DNA cleavage activity. In contrast, the results of mutational analyses and cross-link experiments show that PspGI and SsoII have a very similar DNA binding site and catalytic center as NgoMIV and Cfr10I (whose crystal structures are known), and presumably also as EcoRII, in spite of the fact that these enzymes, which all recognize variants of the sequence -/CC-GG- (/ denotes the site of cleavage), are representatives of different subgroups of type II restriction endonucleases. A sequence comparison of all known restriction endonuclease sequences, furthermore, suggests that several enzymes recognizing other DNA sequences also share amino acid sequence similarities with PspGI, SsoII and EcoRII in the region of the presumptive active site. These results are discussed in an evolutionary context.

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Sprache(n): eng - English
 Datum: 2003-06-20
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 173725
ISI: 000183671600007
DOI: 10.1016/S0022-2836(03)00523-0
 Art des Abschluß: -

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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 329 (5) Artikelnummer: - Start- / Endseite: 913 - 929 Identifikator: ISSN: 0022-2836