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Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus.
Biochemistry. 1995 Jul 04; 34(26):8441-8.B

Abstract

The secondary and quaternary structures and stabilities of recombinant (r) forms of the HMfA and HMfB histones from Methanothermus fervidus have been investigated by CD spectroscopy and formaldehyde-mediated protein-protein cross-linking. Both proteins were shown to be dimers in solutions containing 5-1300 mM KCl, at pH 6-10 and 25-83 degrees C, and specifically in 1 M KCl, at pH 7.5 and 83 degrees C, conditions which approximate those in vivo in M. fervidus cells. Heat treatment of a mixture of rHMfA and rHMfB homodimers resulted in the formation of rHMfA.rHMfB heterodimers, as demonstrated by two-dimensional PAGE. Heterodimer formation did not result in a CD-detectable conformational change from the homodimer states, indicating that homogeneous (rHMfA)2 and (rHMfB)2 preparations may be considered as structural models of heterodimers. At pH 2, both rHMfA and rHMfB were denatured under low-salt (< 0.2 M KCl) conditions, and their conformations were stabilized in a cooperative manner by increasing KCl concentration, with cooperativity constants for KCl uptake of 2.7 and 3.1, respectively. The alpha-helical conformations of rHMfA and rHMfB were salt-dependent, at both pH 2 and pH 7.5, with maximal helicities in 1 M KCl of 84% and 63% at pH 2, and 72% and 65% at pH 7.5, respectively. The data obtained indicate that the structures of HMfA and HMfB, in 100-200 mM KCl at pH 7.5 and 25 degrees C, are likely to be very similar to their in vivo structures, even though these conditions are far removed from those found in vivo.(

ABSTRACT

TRUNCATED AT 250 WORDS)

Authors+Show Affiliations

Department of Microbiology, Ohio State University, Columbus 43210, USA.No 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

7599135

Citation

Grayling, R A., et al. "Structure and Stability of Histone HMf From the Hyperthermophilic Archaeon Methanothermus Fervidus." Biochemistry, vol. 34, no. 26, 1995, pp. 8441-8.
Grayling RA, Becktel WJ, Reeve JN. Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus. Biochemistry. 1995;34(26):8441-8.
Grayling, R. A., Becktel, W. J., & Reeve, J. N. (1995). Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus. Biochemistry, 34(26), 8441-8.
Grayling RA, Becktel WJ, Reeve JN. Structure and Stability of Histone HMf From the Hyperthermophilic Archaeon Methanothermus Fervidus. Biochemistry. 1995 Jul 4;34(26):8441-8. PubMed PMID: 7599135.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus. AU - Grayling,R A, AU - Becktel,W J, AU - Reeve,J N, PY - 1995/7/4/pubmed PY - 1995/7/4/medline PY - 1995/7/4/entrez SP - 8441 EP - 8 JF - Biochemistry JO - Biochemistry VL - 34 IS - 26 N2 - The secondary and quaternary structures and stabilities of recombinant (r) forms of the HMfA and HMfB histones from Methanothermus fervidus have been investigated by CD spectroscopy and formaldehyde-mediated protein-protein cross-linking. Both proteins were shown to be dimers in solutions containing 5-1300 mM KCl, at pH 6-10 and 25-83 degrees C, and specifically in 1 M KCl, at pH 7.5 and 83 degrees C, conditions which approximate those in vivo in M. fervidus cells. Heat treatment of a mixture of rHMfA and rHMfB homodimers resulted in the formation of rHMfA.rHMfB heterodimers, as demonstrated by two-dimensional PAGE. Heterodimer formation did not result in a CD-detectable conformational change from the homodimer states, indicating that homogeneous (rHMfA)2 and (rHMfB)2 preparations may be considered as structural models of heterodimers. At pH 2, both rHMfA and rHMfB were denatured under low-salt (< 0.2 M KCl) conditions, and their conformations were stabilized in a cooperative manner by increasing KCl concentration, with cooperativity constants for KCl uptake of 2.7 and 3.1, respectively. The alpha-helical conformations of rHMfA and rHMfB were salt-dependent, at both pH 2 and pH 7.5, with maximal helicities in 1 M KCl of 84% and 63% at pH 2, and 72% and 65% at pH 7.5, respectively. The data obtained indicate that the structures of HMfA and HMfB, in 100-200 mM KCl at pH 7.5 and 25 degrees C, are likely to be very similar to their in vivo structures, even though these conditions are far removed from those found in vivo.(ABSTRACT TRUNCATED AT 250 WORDS) SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/7599135/Structure_and_stability_of_histone_HMf_from_the_hyperthermophilic_archaeon_Methanothermus_fervidus_ L2 - https://antibodies.cancer.gov/detail/CPTC-CTLA4-1 DB - PRIME DP - Unbound Medicine ER -