THE ELEMENTARY RNP FIBER - NOT THE HIGHER-ORDER STRUCTURE - DETERMINES THE ALL-OR-NONE DISINTEGRATION BEHAVIOR OF BALBIANI RING PREMESSENGER RNP PARTICLES UPON RNASE-A TREATMENT
K. Alexciev et al., THE ELEMENTARY RNP FIBER - NOT THE HIGHER-ORDER STRUCTURE - DETERMINES THE ALL-OR-NONE DISINTEGRATION BEHAVIOR OF BALBIANI RING PREMESSENGER RNP PARTICLES UPON RNASE-A TREATMENT, Biology of the cell, 77(2), 1993, pp. 165-172
Balbiani ring premessenger ribonucleoprotein (RNP) particles are built
from a 7-nm RNP fiber which is tightly folded into a ring-shaped RNP
ribbon. Isolated particles are known to disintegrate in an all-or-none
fashion upon RNase A treatment. In the present study we investigated
whether this mode of disintegration is dependent on an intact particle
structure or is inherent in the 7-nm fiber. When treated at low ionic
strength, the Balbiani ring (BR) particles lost their higher order st
ructure and the 7-nm fiber was unpacked, as evidenced by sucrose gradi
ent sedimentation and electron microscopy. When treated with RNase A,
unfolded as well as intact particles disintegrated in the all-or-none
fashion, with similar kinetics and without apparent intermediates. Pro
teinase K treatment, however, obliterated this pattern: the protein-fr
ee particle RNA degraded progressively. As the typical disintegration
pattern of the particles was not altered by unfolding, but was lost by
deproteinization, the all-or-none mode of disintegration is likely to
be a property of the 7-nm RNP fiber.