Binding of TmHU to single dsDNA as observed by optical tweezers.
Optical tweezers are employed to study the action of the histone-like protein from Thermotoga maritima (TmHU) on DNA at a single molecule level. Binding and disruption of TmHU to and from DNA are found to take place in discrete steps of 4-5 nm length and a net binding enthalpy of about 16kBT. This is in reasonable agreement with a microscopic model that estimates the extension of the binding sites of the protein and evaluates the energetics mainly for bending of the DNA in the course of interaction.
Salomo
M
M
Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, Brüderstrasse 34, D-04103 Leipzig, Germany.
Kroy
K
K
Kegler
K
K
Gutsche
C
C
Struhalla
M
M
Reinmuth
J
J
Skokov
W
W
Immisch
C
C
Hahn
U
U
Kremer
F
F
D001426:Bacterial Proteins / Q000737:chemistry*; D004247:DNA / Q000737:chemistry*; D004277:DNA, Single-Stranded / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry*; D008958:Models, Molecular; D055095:Optics and Photonics; D011485:Protein Binding; D011487:Protein Conformation; D020124:Thermotoga maritima / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; C040330:histone-like protein HU, bacteria; D004247:DNA