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http://purl.uniprot.org/citations/2377617http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2377617http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2377617http://www.w3.org/2000/01/rdf-schema#comment"Methanothermus fervidus grows optimally at 83 degrees C. A protein designated HMf (histone M. fervidus) has been isolated from this archaeal hyperthermophile that binds to double-stranded DNA molecules and increases their resistance to thermal denaturation. HMf binding to linear double-stranded DNA molecules of greater than 2 kilobase pairs also increases their electrophoretic mobilities through agarose gels. Visualization of this compaction process by electron microscopy has demonstrated the formation of quasispherical, macromolecular HMf-DNA complexes. HMf is a mixture of approximately equal amounts of two very similar polypeptides designated HMf-1 and HMf-2. Determination of the DNA sequence of the gene encoding HMf-2 (hmfB) has revealed that over 30% of the amino acid residues in HMf-2 are conserved in the consensus sequences derived for eucaryal histones H2A, H2B, H3, and H4. These archaeal polypeptides and eucaryal histones appear therefore to have evolved from a common ancestor and are likely to have related structures and functions."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.org/dc/terms/identifier"doi:10.1073/pnas.87.15.5788"xsd:string
http://purl.uniprot.org/citations/2377617http://purl.org/dc/terms/identifier"doi:10.1073/pnas.87.15.5788"xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Lurz R."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Lurz R."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Krzycki J.A."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Krzycki J.A."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Reeve J.N."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Reeve J.N."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Sandman K."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Sandman K.M."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Sandman K.M."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Dobrinski B."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/author"Dobrinski B."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/pages"5788-5791"xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/pages"5788-5791"xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/title"HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/title"HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones."xsd:string
http://purl.uniprot.org/citations/2377617http://purl.uniprot.org/core/volume"87"xsd:string