منابع مشابه
Histone H1 gets Pin’d onto chromatin
Histone H1 gets Pin'd onto chromatin T he proline isomerase Pin1 limits chromosome decon-densation by stabilizing a histone's association with chromatin, Raghuram et al. reveal. Histone H1 incorporates into nucleosomes to enhance chromatin folding and condensation. Phosphory-lation by the cyclin-dependent kinase Cdk2 promotes H1's dissociation from chromatin, perhaps by altering the conformatio...
متن کاملDistribution of H1 histone in chromatin digested by micrococcal nuclease.
The relative amount of H1 histone associated with isolated nucleosomes from calf thymus was determined as a function of the extent of DNA digestion by micrococcal nuclease. Generally the amount of H1 histone associated with mononucleosomes decreases with increasing digestion until 60% of the original H1 remains associated with DNA 150 base pirs or less in size. Coincidentally, H1 histone increa...
متن کاملHistone H1 compacts DNA under force and during chromatin assembly
Histone H1 binds to linker DNA between nucleosomes, but the dynamics and biological ramifications of this interaction remain poorly understood. We performed single-molecule experiments using magnetic tweezers to determine the effects of H1 on naked DNA in buffer or during chromatin assembly in Xenopus egg extracts. In buffer, nanomolar concentrations of H1 induce bending and looping of naked DN...
متن کاملChromatin structure: Linking structure to function with histone H1
A recent study has determined the position and orientation in the nucleosome of the H1 variant 'linker histone' H5; the results focus attention on the unknown function of this highly abundant nuclear protein, and highlight the question of whether H1 is primarily an architectural or a gene-regulatory protein.
متن کاملProthymosin alpha modulates the interaction of histone H1 with chromatin
Prothymosin alpha (ProTalpha) is an abundant acidic nuclear protein that may be involved in cell proliferation. In our search for its cellular partners, we have recently found that ProTalpha binds to linker histone H1. We now provide further evidence for the physiological relevance of this interaction by immunoisolation of a histone H1-ProTalpha complex from NIH 3T3 cell extracts. A detailed an...
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: Journal of Cell Biology
سال: 2013
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.2031iti1