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DNA binding and nuclease protection by the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus.
Extremophiles. 1997 May; 1(2):79-88.E

Abstract

The DNA-binding and nuclease-protection properties of the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus have been shown to be consistent with the formation of nucleosome-like structures (NLS). These proteins bind to DNA molecules as short as 20 bp and form complexes that protect DNA fragments from micrococcal nuclease (MNase) digestion that are 30 bp, approximately 60 bp and multiples of approximately 60 bp in length. The sequences of 49 of the approximately 60-bp DNA fragments protected from MNase digestion by HMfA have been determined and their intrinsic curvatures calculated. A circular permutation gel mobility-shift assay was used to determine directly the curvatures for five of these sequences. HMfA bound to intrinsically curved and noncurved DNAs, but exhibited a slight preference for the model curved DNA in binding competitions with a model noncurved DNA. The results obtained are consistent with the concept that the archaeal NLS is analogous, and possibly homologous, to the central core of the eukaryal nucleosome formed by a histone (H3 + H4)2 tetramer.

Authors+Show Affiliations

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

Pub Type(s)

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

Language

eng

PubMed ID

9680306

Citation

Grayling, R A., et al. "DNA Binding and Nuclease Protection By the HMf Histones From the Hyperthermophilic Archaeon Methanothermus Fervidus." Extremophiles : Life Under Extreme Conditions, vol. 1, no. 2, 1997, pp. 79-88.
Grayling RA, Bailey KA, Reeve JN. DNA binding and nuclease protection by the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus. Extremophiles. 1997;1(2):79-88.
Grayling, R. A., Bailey, K. A., & Reeve, J. N. (1997). DNA binding and nuclease protection by the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus. Extremophiles : Life Under Extreme Conditions, 1(2), 79-88.
Grayling RA, Bailey KA, Reeve JN. DNA Binding and Nuclease Protection By the HMf Histones From the Hyperthermophilic Archaeon Methanothermus Fervidus. Extremophiles. 1997;1(2):79-88. PubMed PMID: 9680306.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - DNA binding and nuclease protection by the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus. AU - Grayling,R A, AU - Bailey,K A, AU - Reeve,J N, PY - 1997/5/1/pubmed PY - 1998/7/29/medline PY - 1997/5/1/entrez SP - 79 EP - 88 JF - Extremophiles : life under extreme conditions JO - Extremophiles VL - 1 IS - 2 N2 - The DNA-binding and nuclease-protection properties of the HMf histones from the hyperthermophilic archaeon Methanothermus fervidus have been shown to be consistent with the formation of nucleosome-like structures (NLS). These proteins bind to DNA molecules as short as 20 bp and form complexes that protect DNA fragments from micrococcal nuclease (MNase) digestion that are 30 bp, approximately 60 bp and multiples of approximately 60 bp in length. The sequences of 49 of the approximately 60-bp DNA fragments protected from MNase digestion by HMfA have been determined and their intrinsic curvatures calculated. A circular permutation gel mobility-shift assay was used to determine directly the curvatures for five of these sequences. HMfA bound to intrinsically curved and noncurved DNAs, but exhibited a slight preference for the model curved DNA in binding competitions with a model noncurved DNA. The results obtained are consistent with the concept that the archaeal NLS is analogous, and possibly homologous, to the central core of the eukaryal nucleosome formed by a histone (H3 + H4)2 tetramer. SN - 1431-0651 UR - https://www.unboundmedicine.com/medline/citation/9680306/DNA_binding_and_nuclease_protection_by_the_HMf_histones_from_the_hyperthermophilic_archaeon_Methanothermus_fervidus_ DB - PRIME DP - Unbound Medicine ER -