Tags

Type your tag names separated by a space and hit enter

Solution structure, stability, and nucleic acid binding of the hyperthermophile protein Sso10b2.
Biochemistry. 2005 Nov 01; 44(43):14217-30.B

Abstract

The Sso10b (or Alba) family of proteins is a conserved group of archaeal and eukaryotic proteins which are thought to play a role in both chromatin organization and RNA metabolism. We describe here the solution structure and properties of Sso10b2 from Sulfolobus solfataricus. NMR data including residual dipolar couplings and (15)N relaxation data demonstrated that the protein adopts a beta(1)alpha(1)beta(2)alpha(2)beta(3)beta(4) topology with an IF-3-like fold. The protein dimerizes in solution at 30 degrees C via a hydrophobic surface defined by the C-terminal alpha(2)beta(3)beta(4) elements with a structure similar to one of the putative dimers indicated by previous crystal structures. DSC and circular dichroism data demonstrated an unusual two-state structural transition near the growth temperature which led to an increase in beta-sheet content without dissociation of the dimer. The cooperativity of the transition exceeded that of a dimer at pH 7, demonstrating the presence of higher order oligomers near the growth temperature at pH 7. Reverse titrations of Sso10b2 with nucleic acid showed that the protein binds single-stranded DNA (K(d) of 3 x 10(-)(7) M) with higher affinity than RNA (1.3 x 10(-)(6) M) or double-stranded DNA (1.5 x 10(-)(5) M) in 10 mM KH(2)PO(4) (pH 7.0, 20 degrees C). NMR chemical shift perturbation data indicated that single-stranded DNA and RNA binding occurred across the same dimer interface and encompassed a surface defined by the C-terminal ends of the beta(1), beta(2), and beta(3) strands of each monomer.

Authors+Show Affiliations

Laboratory for Structural Biology, Department of Chemistry, Graduate Program in Biotechnology and Bioengineering, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

16245938

Citation

Biyani, Kalpesh, et al. "Solution Structure, Stability, and Nucleic Acid Binding of the Hyperthermophile Protein Sso10b2." Biochemistry, vol. 44, no. 43, 2005, pp. 14217-30.
Biyani K, Kahsai MA, Clark AT, et al. Solution structure, stability, and nucleic acid binding of the hyperthermophile protein Sso10b2. Biochemistry. 2005;44(43):14217-30.
Biyani, K., Kahsai, M. A., Clark, A. T., Armstrong, T. L., Edmondson, S. P., & Shriver, J. W. (2005). Solution structure, stability, and nucleic acid binding of the hyperthermophile protein Sso10b2. Biochemistry, 44(43), 14217-30.
Biyani K, et al. Solution Structure, Stability, and Nucleic Acid Binding of the Hyperthermophile Protein Sso10b2. Biochemistry. 2005 Nov 1;44(43):14217-30. PubMed PMID: 16245938.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Solution structure, stability, and nucleic acid binding of the hyperthermophile protein Sso10b2. AU - Biyani,Kalpesh, AU - Kahsai,Mebrahtu A, AU - Clark,Andrew T, AU - Armstrong,Tracy L, AU - Edmondson,Stephen P, AU - Shriver,John W, PY - 2005/10/26/pubmed PY - 2006/1/28/medline PY - 2005/10/26/entrez SP - 14217 EP - 30 JF - Biochemistry JO - Biochemistry VL - 44 IS - 43 N2 - The Sso10b (or Alba) family of proteins is a conserved group of archaeal and eukaryotic proteins which are thought to play a role in both chromatin organization and RNA metabolism. We describe here the solution structure and properties of Sso10b2 from Sulfolobus solfataricus. NMR data including residual dipolar couplings and (15)N relaxation data demonstrated that the protein adopts a beta(1)alpha(1)beta(2)alpha(2)beta(3)beta(4) topology with an IF-3-like fold. The protein dimerizes in solution at 30 degrees C via a hydrophobic surface defined by the C-terminal alpha(2)beta(3)beta(4) elements with a structure similar to one of the putative dimers indicated by previous crystal structures. DSC and circular dichroism data demonstrated an unusual two-state structural transition near the growth temperature which led to an increase in beta-sheet content without dissociation of the dimer. The cooperativity of the transition exceeded that of a dimer at pH 7, demonstrating the presence of higher order oligomers near the growth temperature at pH 7. Reverse titrations of Sso10b2 with nucleic acid showed that the protein binds single-stranded DNA (K(d) of 3 x 10(-)(7) M) with higher affinity than RNA (1.3 x 10(-)(6) M) or double-stranded DNA (1.5 x 10(-)(5) M) in 10 mM KH(2)PO(4) (pH 7.0, 20 degrees C). NMR chemical shift perturbation data indicated that single-stranded DNA and RNA binding occurred across the same dimer interface and encompassed a surface defined by the C-terminal ends of the beta(1), beta(2), and beta(3) strands of each monomer. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/16245938/Solution_structure_stability_and_nucleic_acid_binding_of_the_hyperthermophile_protein_Sso10b2_ L2 - https://doi.org/10.1021/bi051266r DB - PRIME DP - Unbound Medicine ER -