Mechanism of DNA flexibility enhancement by HMGB proteins
نویسندگان
چکیده
منابع مشابه
Mechanism of DNA flexibility enhancement by HMGB proteins
The mechanism by which sequence non-specific DNA-binding proteins enhance DNA flexibility is studied by examining complexes of double-stranded DNA with the high mobility group type B proteins HMGB2 (Box A) and HMGB1 (Box A+B) using atomic force microscopy. DNA end-to-end distances and local DNA bend angle distributions are analyzed for protein complexes deposited on a mica surface. For HMGB2 (B...
متن کاملSingle-molecule kinetics reveal microscopic mechanism by which High-Mobility Group B proteins alter DNA flexibility
Eukaryotic High-Mobility Group B (HMGB) proteins alter DNA elasticity while facilitating transcription, replication and DNA repair. We developed a new single-molecule method to probe non-specific DNA interactions for two HMGB homologs: the human HMGB2 box A domain and yeast Nhp6Ap, along with chimeric mutants replacing neutral N-terminal residues of the HMGB2 protein with cationic sequences fro...
متن کاملProtein flexibility directs DNA recognition by the papillomavirus E2 proteins
Although DNA flexibility is known to play an important role in DNA-protein interactions, the importance of protein flexibility is less well understood. Here, we show that protein dynamics are important in DNA recognition using the well-characterized human papillomavirus (HPV) type 6 E2 protein as a model system. We have compared the DNA binding properties of the HPV 6 E2 DNA binding domain (DBD...
متن کاملFouling Mechanism Study of Nanoporous Membrane by Ultrafitration of Whey Proteins
One of the barriers during whey filtration using UF membrane is the fouling phenomenon of the membrane, which is caused by whey proteins. In this work, the UF membranes were prepared using polysufone (PSf), dimethyl formamide (DMF), 1 wt.% poly vinyl pyrrolidone (PVP) and different concentrations of LiCl via phase inversion induced by immersion precipitation. The prepared membranes were charact...
متن کاملElectrostatic mechanism for DNA bending by bZIP proteins.
Biology is replete with examples of protein-induced DNA bending, yet the forces responsible for bending have been neither established nor quantified. Mirzabekov and Rich proposed in 1979 that asymmetric neutralization of the anionic phosphodiester backbone by basic histone proteins could provide a thermodynamic driving force for DNA bending in the nucleosome core particle [Mirzabekov, A. D., & ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2009
ISSN: 1362-4962,0305-1048
DOI: 10.1093/nar/gkn1011