HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines.
HMf, a histone-related protein from Methanothermus fervidus, was found to bind preferentially to a DNA that is intrinsically bent as a result of the presence of phased oligo(dA) tracts. The intergenic regions in M. fervidus DNA are A+T rich and frequently contain oligo(dA) tracts, some of which may have the size and phasing required to create a net bending in one direction. The binding of HMf to bent DNA could play a direct role in gene expression and stabilization of the genome of this organism.
Howard
M T
MT
Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill 27599.
Sandman
K
K
Reeve
J N
JN
Griffith
J D
JD
D019843:Archaeal Proteins; D001482:Base Composition; D004269:DNA, Bacterial / Q000378:metabolism* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000378:metabolism*; D019605:Euryarchaeota / Q000737:chemistry*; D006657:Histones; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides / Q000378:metabolism*; D010957:Plasmids / Q000648:ultrastructure; D015183:Restriction Mapping
D019843:Archaeal Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; C065108:HMf protein, Archaeal; D006657:Histones; D009838:Oligodeoxyribonucleotides; C030570:oligodeoxyadenylic acid