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DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus.
J Mol Biol. 1995 Apr 14; 247(5):840-6.JM

Abstract

We have used nuclear magnetic resonance (n.m.r.) spectroscopy to identify the DNA-binding surface of the abundant, small and basic protein Sso7d from the hyperthermophilic archaebacterium Sulfolobus solfataricus. The Sso7d protein was previously found to bind strongly to double-stranded DNA sequences and to protect DNA from thermal denaturation, indicating that it might assume a similar function in vivo. Several amide resonances in two-dimensional n.m.r. 1H, 15N correlation spectra of 15N-enriched Sso7d are shifted and broadened upon addition of small amounts of ten base-pair or 19 base-pair duplex DNA oligomers under conditions where Sso7d-DNA complexes exchange rapidly on the n.m.r. time scale. The locations of the corresponding amides in the Sso7d structure define the surface that interacts with DNA. This surface coincides with a continuous region of strong positive electrostatic potential, which was calculated by means of numerical solution of the Poisson-Boltzmann equation. A model of the non-specific Sso7d-DNA complex is suggested based on the present data and previously obtained evidence that Sso7d interacts with the DNA major groove. The protein-DNA interface consists of a triple-stranded beta-sheet, which interacts with the DNA major groove and a reverse turn connecting the two strands of a double-stranded beta-sheet, which interacts with the minor groove. We note that the five (of 14) lysine side-chains that are specifically subjected to N zeta-monomethylation in the cell are located on surfaces of Sso7d that are exposed to the solvent in the proposed Sso7d-DNA complex.

Authors+Show Affiliations

Center for Structural Biochemistry, Karolinska Institutet, Novum, Huddinge, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

7723036

Citation

Baumann, H, et al. "DNA-binding Surface of the Sso7d Protein From Sulfolobus Solfataricus." Journal of Molecular Biology, vol. 247, no. 5, 1995, pp. 840-6.
Baumann H, Knapp S, Karshikoff A, et al. DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus. J Mol Biol. 1995;247(5):840-6.
Baumann, H., Knapp, S., Karshikoff, A., Ladenstein, R., & Härd, T. (1995). DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus. Journal of Molecular Biology, 247(5), 840-6.
Baumann H, et al. DNA-binding Surface of the Sso7d Protein From Sulfolobus Solfataricus. J Mol Biol. 1995 Apr 14;247(5):840-6. PubMed PMID: 7723036.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus. AU - Baumann,H, AU - Knapp,S, AU - Karshikoff,A, AU - Ladenstein,R, AU - Härd,T, PY - 1995/4/14/pubmed PY - 1995/4/14/medline PY - 1995/4/14/entrez SP - 840 EP - 6 JF - Journal of molecular biology JO - J Mol Biol VL - 247 IS - 5 N2 - We have used nuclear magnetic resonance (n.m.r.) spectroscopy to identify the DNA-binding surface of the abundant, small and basic protein Sso7d from the hyperthermophilic archaebacterium Sulfolobus solfataricus. The Sso7d protein was previously found to bind strongly to double-stranded DNA sequences and to protect DNA from thermal denaturation, indicating that it might assume a similar function in vivo. Several amide resonances in two-dimensional n.m.r. 1H, 15N correlation spectra of 15N-enriched Sso7d are shifted and broadened upon addition of small amounts of ten base-pair or 19 base-pair duplex DNA oligomers under conditions where Sso7d-DNA complexes exchange rapidly on the n.m.r. time scale. The locations of the corresponding amides in the Sso7d structure define the surface that interacts with DNA. This surface coincides with a continuous region of strong positive electrostatic potential, which was calculated by means of numerical solution of the Poisson-Boltzmann equation. A model of the non-specific Sso7d-DNA complex is suggested based on the present data and previously obtained evidence that Sso7d interacts with the DNA major groove. The protein-DNA interface consists of a triple-stranded beta-sheet, which interacts with the DNA major groove and a reverse turn connecting the two strands of a double-stranded beta-sheet, which interacts with the minor groove. We note that the five (of 14) lysine side-chains that are specifically subjected to N zeta-monomethylation in the cell are located on surfaces of Sso7d that are exposed to the solvent in the proposed Sso7d-DNA complex. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/7723036/DNA_binding_surface_of_the_Sso7d_protein_from_Sulfolobus_solfataricus_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(85)70184-2 DB - PRIME DP - Unbound Medicine ER -