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  Crystal structure of a novel domain of the motor subunit of the Type I restriction enzyme EcoR124 involved in complex assembly and DNA binding

Grinkevich, P., Sinha, D., Iermak, I., Guzanova, A., Weiserova, M., Ludwig, J., et al. (2018). Crystal structure of a novel domain of the motor subunit of the Type I restriction enzyme EcoR124 involved in complex assembly and DNA binding. The Journal of Biological Chemistry, 293(39), 15043-15054. doi:10.1074/jbc.RA118.003978.

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J. Biol. Chem.-2018-Grinkevich-15043-54.pdf (Verlagsversion), 4MB
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 Urheber:
Grinkevich, Pavel1, Autor
Sinha, Dhiraj1, Autor
Iermak, Iuliia2, Autor           
Guzanova, Alena1, Autor
Weiserova, Marie1, Autor
Ludwig, Jost1, Autor
Mesters, Jeroen R.1, Autor
Ettrich, Ruediger H.1, Autor
Affiliations:
1external, ou_persistent22              
2Biertümpfel, Christian / Molecular Mechanisms of DNA Repair, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565143              

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Schlagwörter: VIBRIO-VULNIFICUS YJ016; ESCHERICHIA-COLI; MODIFICATION SYSTEM; HSDR SUBUNIT; SEQUENCE; PROTEIN; GENES; CRYSTALLIZATION; TRANSLOCATION; PURIFICATIONBiochemistry & Molecular Biology; crystal structure; X-ray crystallography; DNA endonuclease; DNA binding protein; Escherichia coli (E; coli); C-terminal domain; EcoR124; GFP fusion; HsdR; restriction-modification;
 Zusammenfassung: Although EcoR124 is one of the better-studied Type I restriction-modification enzymes, it still presents many challenges to detailed analyses because of its structural and functional complexity and missing structural information. In all available structures of its motor subunit HsdR, responsible for DNA translocation and cleavage, a large part of the HsdR C terminus remains unresolved. The crystal structure of the C terminus of HsdR, obtained with a crystallization chaperone in the form of pHluorin fusion and refined to 2.45 , revealed that this part of the protein forms an independent domain with its own hydrophobic core and displays a unique -helical fold. The full-length HsdR model, based on the WT structure and the C-terminal domain determined here, disclosed a proposed DNA-binding groove lined by positively charged residues. In vivo and in vitro assays with a C-terminal deletion mutant of HsdR supported the idea that this domain is involved in complex assembly and DNA binding. Conserved residues identified through sequence analysis of the C-terminal domain may play a key role in protein-protein and protein-DNA interactions. We conclude that the motor subunit of EcoR124 comprises five structural and functional domains, with the fifth, the C-terminal domain, revealing a unique fold characterized by four conserved motifs in the IC subfamily of Type I restriction-modification systems. In summary, the structural and biochemical results reported here support a model in which the C-terminal domain of the motor subunit HsdR of the endonuclease EcoR124 is involved in complex assembly and DNA binding.

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Sprache(n): eng - English
 Datum: 2018-072018
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000445998400009
DOI: 10.1074/jbc.RA118.003978
 Art des Abschluß: -

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Titel: The Journal of Biological Chemistry
  Andere : JBC
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 293 (39) Artikelnummer: - Start- / Endseite: 15043 - 15054 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1