Health & Wellness - March 2012 Archives

JACKSONVILLE, Flórida — Pesquisadores identificaram um gene que causa a distonia cervical primária, contraída no início da vida adulta, frequentemente dolorosa, em que o pescoço ...

Benefits of Osteopenia Medication Remain Even After Discontinuing Use March 9, 2012 Dear Mayo Clinic: If I have taken a bisphosphonate for five years, ...

Seems fitting that National Sleep Awareness Week should end on Sunday March 11th, when we 'technically' lose an hour of sleep.  Daylight Saving Time means moving our ...

Epilepsy affects approximately 1 percent of the human population, with an estimated 50 million people worldwide currently suffering from the disorder. The hallmark of epilepsy ...

ROCHESTER, Minn. — Mayo Clinic researchers this week will announce the use of the blood pressure drug prazosin as an effective treatment to curb post-traumatic ...

On July 16, 1999 John Kennedy Jr. died when the plane he was piloting crashed into the Atlantic Ocean off Martha’s Vineyard. Experts suspect Kennedy ...

History of Baldness on Either Side of Family Increases Risk of Balding March 2, 2012 Dear Mayo Clinic: Is it true that you ...

For patients diagnosed with myelofibrosis, a bone marrow disorder that disrupts the body’s normal production of blood cells, new hope may be on the horizon. A ...

ROCHESTER, Minn. — Mayo Clinic researchers have gained insights into the function of a member of a family of specialized proteins called histone chaperones. Using nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, they have determined the 3-D structure and interactions of the histone chaperone Rtt106 down to the atomic details. The findings are published in the journal Nature. "The interactions we described are important for gene silencing and the DNA damage response," says senior author Georges Mer, Ph.D., a Mayo Clinic structural biologist. "This is exciting because our newfound knowledge will help us better understand these fundamental cellular processes." In cells, our DNA is part of a structure called chromatin, comprised of proteins, the majority called histones, which are wrapped with the DNA. Associated with the histones is another group of proteins called histone chaperones, which promote the proper assembly or disassembly of the chromatin during the times our DNA is replicated or repaired when damaged. Their dysfunction has been linked to cancer, aging and other diseases. The Discovery Before this Mayo study, scientists knew that the histone chaperone Rtt106 helped in the deposition of histones — specifically, a complex of histones H3 and H4 — onto the replicating DNA. They did not understand how Rtt106 does this, given that it does not possess any of the known requirements. Histone H3 is in a modified form where one of its amino acids, lysine 56, is acetylated. Rtt106 does not seem to have an acetylated lysine reader domain.