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HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines.
J Bacteriol. 1992 Dec; 174(23):7864-7.JB

Abstract

HMf, a histone-related protein from Methanothermus fervidus, was found to bind preferentially to a DNA that is intrinsically bent as a result of the presence of phased oligo(dA) tracts. The intergenic regions in M. fervidus DNA are A+T rich and frequently contain oligo(dA) tracts, some of which may have the size and phasing required to create a net bending in one direction. The binding of HMf to bent DNA could play a direct role in gene expression and stabilization of the genome of this organism.

Authors+Show Affiliations

Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill 27599.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

1447158

Citation

Howard, M T., et al. "HMf, a Histone-related Protein From the Hyperthermophilic Archaeon Methanothermus Fervidus, Binds Preferentially to DNA Containing Phased Tracts of Adenines." Journal of Bacteriology, vol. 174, no. 23, 1992, pp. 7864-7.
Howard MT, Sandman K, Reeve JN, et al. HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines. J Bacteriol. 1992;174(23):7864-7.
Howard, M. T., Sandman, K., Reeve, J. N., & Griffith, J. D. (1992). HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines. Journal of Bacteriology, 174(23), 7864-7.
Howard MT, et al. HMf, a Histone-related Protein From the Hyperthermophilic Archaeon Methanothermus Fervidus, Binds Preferentially to DNA Containing Phased Tracts of Adenines. J Bacteriol. 1992;174(23):7864-7. PubMed PMID: 1447158.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines. AU - Howard,M T, AU - Sandman,K, AU - Reeve,J N, AU - Griffith,J D, PY - 1992/12/1/pubmed PY - 1992/12/1/medline PY - 1992/12/1/entrez SP - 7864 EP - 7 JF - Journal of bacteriology JO - J Bacteriol VL - 174 IS - 23 N2 - HMf, a histone-related protein from Methanothermus fervidus, was found to bind preferentially to a DNA that is intrinsically bent as a result of the presence of phased oligo(dA) tracts. The intergenic regions in M. fervidus DNA are A+T rich and frequently contain oligo(dA) tracts, some of which may have the size and phasing required to create a net bending in one direction. The binding of HMf to bent DNA could play a direct role in gene expression and stabilization of the genome of this organism. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/1447158/HMf_a_histone_related_protein_from_the_hyperthermophilic_archaeon_Methanothermus_fervidus_binds_preferentially_to_DNA_containing_phased_tracts_of_adenines_ L2 - https://journals.asm.org/doi/10.1128/jb.174.23.7864-7867.1992?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -