Tags

Type your tag names separated by a space and hit enter

Biochemical characterization and helix stabilizing properties of HSNP-C' from the thermoacidophilic archaeon Sulfolobus acidocaldarius.
Biochem Biophys Res Commun. 2000 Jan 19; 267(2):614-8.BB

Abstract

Helix stabilizing nucleoid protein HSNP-C' from the thermophilic archaeon Sulfolobus acidocaldarius has been characterized with respect to its interactions with nucleic acids by gel retardation assay, affinities to immobilized matrices, electron microscopy, and fluorescence titration. The amino acids implicated in the DNA binding site of the protein have been shown by selectively modifying specific amino acyl functional groups and looking at their effects on the DNA binding properties of the protein. Lysine, arginine, tryptophan, and tyrosine residues of the protein HSNP-C' were modified with pyridoxal-5-phosphate; 2,3-butanedione; BNPS-skatole; and tetranitromethane, respectively. The modification of residues was assessed according to standard procedures. The effect of the chemical modification on the function of the protein HSNP-C' with respect to DNA protein interactions was studied and the results indicate the definite involvement of tyrosines and also the significant involvement of the flanking tryptophan residues in the DNA binding domain on the protein.

Links

Publisher Full Text

Authors+Show Affiliations

Celestina F
Department of Biochemistry, University of Hyderabad, Hyderabad, 500046, India. Francina_Celestina@urmc.rochester.edu
Suryanarayana T
No affiliation info available

MeSH

Amino AcidsArchaeal ProteinsBinding SitesDNA, ArchaealDNA-Binding ProteinsHot TemperatureNucleic Acid ConformationNucleic Acid DenaturationSpectrophotometrySulfolobus acidocaldariusTryptophanTyrosine

Pub Type(s)

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

Language

eng

PubMed ID

10631111

Citation

Celestina, F, and T Suryanarayana. "Biochemical Characterization and Helix Stabilizing Properties of HSNP-C' From the Thermoacidophilic Archaeon Sulfolobus Acidocaldarius." Biochemical and Biophysical Research Communications, vol. 267, no. 2, 2000, pp. 614-8.
Celestina F, Suryanarayana T. Biochemical characterization and helix stabilizing properties of HSNP-C' from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Biochem Biophys Res Commun. 2000;267(2):614-8.
Celestina, F., & Suryanarayana, T. (2000). Biochemical characterization and helix stabilizing properties of HSNP-C' from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Biochemical and Biophysical Research Communications, 267(2), 614-8.
Celestina F, Suryanarayana T. Biochemical Characterization and Helix Stabilizing Properties of HSNP-C' From the Thermoacidophilic Archaeon Sulfolobus Acidocaldarius. Biochem Biophys Res Commun. 2000 Jan 19;267(2):614-8. PubMed PMID: 10631111.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical characterization and helix stabilizing properties of HSNP-C' from the thermoacidophilic archaeon Sulfolobus acidocaldarius. AU - Celestina,F, AU - Suryanarayana,T, PY - 2000/1/13/pubmed PY - 2000/2/26/medline PY - 2000/1/13/entrez SP - 614 EP - 8 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 267 IS - 2 N2 - Helix stabilizing nucleoid protein HSNP-C' from the thermophilic archaeon Sulfolobus acidocaldarius has been characterized with respect to its interactions with nucleic acids by gel retardation assay, affinities to immobilized matrices, electron microscopy, and fluorescence titration. The amino acids implicated in the DNA binding site of the protein have been shown by selectively modifying specific amino acyl functional groups and looking at their effects on the DNA binding properties of the protein. Lysine, arginine, tryptophan, and tyrosine residues of the protein HSNP-C' were modified with pyridoxal-5-phosphate; 2,3-butanedione; BNPS-skatole; and tetranitromethane, respectively. The modification of residues was assessed according to standard procedures. The effect of the chemical modification on the function of the protein HSNP-C' with respect to DNA protein interactions was studied and the results indicate the definite involvement of tyrosines and also the significant involvement of the flanking tryptophan residues in the DNA binding domain on the protein. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/10631111/Biochemical_characterization_and_helix_stabilizing_properties_of_HSNP_C'_from_the_thermoacidophilic_archaeon_Sulfolobus_acidocaldarius_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(99)92005-3 DB - PRIME DP - Unbound Medicine ER -