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HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones.
Proc Natl Acad Sci U S A. 1990 Aug; 87(15):5788-91.PN

Abstract

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.

Authors+Show Affiliations

Department of Microbiology, Ohio State University, Columbus 43210.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

2377617

Citation

Sandman, K, et al. "HMf, a DNA-binding Protein Isolated From the Hyperthermophilic Archaeon Methanothermus Fervidus, Is Most Closely Related to Histones." Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 15, 1990, pp. 5788-91.
Sandman K, Krzycki JA, Dobrinski B, et al. HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proc Natl Acad Sci U S A. 1990;87(15):5788-91.
Sandman, K., Krzycki, J. A., Dobrinski, B., Lurz, R., & Reeve, J. N. (1990). HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proceedings of the National Academy of Sciences of the United States of America, 87(15), 5788-91.
Sandman K, et al. HMf, a DNA-binding Protein Isolated From the Hyperthermophilic Archaeon Methanothermus Fervidus, Is Most Closely Related to Histones. Proc Natl Acad Sci U S A. 1990;87(15):5788-91. PubMed PMID: 2377617.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. AU - Sandman,K, AU - Krzycki,J A, AU - Dobrinski,B, AU - Lurz,R, AU - Reeve,J N, PY - 1990/8/1/pubmed PY - 1990/8/1/medline PY - 1990/8/1/entrez SP - 5788 EP - 91 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 87 IS - 15 N2 - 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. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/2377617/HMf_a_DNA_binding_protein_isolated_from_the_hyperthermophilic_archaeon_Methanothermus_fervidus_is_most_closely_related_to_histones_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=2377617 DB - PRIME DP - Unbound Medicine ER -