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...
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The high-mobility-group B (HMGB) chromosomal proteins are characterized by the HMG box, a DNA-binding domain that both introduces a tight bend into DNA and binds preferentially to a variety of distorted DNA structures. The HMGB proteins seem to act primarily as architectural facilitators in the manipulation of nucleoprotein complexes; for example, in the assembly of complexes involved in recomb...
متن کاملEukaryotic HMGB proteins as replacements for HU in E. coli repression loop formation
DNA looping is important for gene repression and activation in Escherichia coli and is necessary for some kinds of gene regulation and recombination in eukaryotes. We are interested in sequence-nonspecific architectural DNA-binding proteins that alter the apparent flexibility of DNA by producing transient bends or kinks in DNA. The bacterial heat unstable (HU) and eukaryotic high-mobility group...
متن کاملSerum and synovial fluid proteins in arthritis.
Synovial fluid is generally considered to be a dialysate of plasma to which mucin has been added during its passage through the synovial membrane (Ropes and Bauer, 1953). The proteins of the serum and synovial fluid have been shown to be qualitatively identical (Schmid and MacNair, 1956) and the concentrations of the various proteins in synovial fluid probably depend upon the following factors:...
متن کاملCitrullinated proteins in rheumatoid arthritis.
Citrullinated proteins that are produced by enzymatic deimination of arginine residues in proteins by peptidylarginine deiminases (PADIs) are of particular interest in the pathogenesis of rheumatoid arthritis (RA). First, peptidylarginine deiminase type 4 (PADI4) gene, which codes one of the PADI enzyme isotypes, has a genetic variant that increases susceptibility to RA. The RA-susceptible vari...
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ژورنال
عنوان ژورنال: Human Cell
سال: 2017
ISSN: 1749-0774
DOI: 10.1007/s13577-017-0182-x