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The formation of higher order protein
Volume 270,
Number 15,
Issue of April 14, pp. 8744-8754, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
CONSEQUENCES FOR NUCLEOPROTEIN COMPLEX ASSEMBLY AND CHROMATIN
CONDENSATION
DNA structures often
requires bending of DNA strands between specific sites, a process that
can be facilitated by the action of nonspecific DNA-binding proteins
which serve as assembly factors. A model for this activity is the
formation of the invertasome, an intermediate structure created in the
Hin-mediated site-specific DNA inversion reaction, which is stimulated
by the prokaryotic nucleoid-associated protein HU. Previously, we have
shown that the mammalian HMG1/2 proteins substitute for HU in this
system and display efficient DNA wrapping activity in vitro.
In the present work, we isolate the primary sources of assembly factor
activity in Saccharomyces cerevisiae, as measured by the
ability to stimulate invertasome formation, and show that these are the
previously identified NHP6A/B proteins. NHP6A/B have comparable or
greater activity in DNA binding, bending, and supercoiling with respect
to HU and HMG1 and appear to form more stable protein
DNA
complexes. In addition, expression of NHP6A in mutant Escherichia
coli cells lacking HU and Fis restores normal morphological
appearance to these cells, specifically in nucleoid condensation and
segregation. From these data we predict diverse architectural roles for
NHP6A/B in manipulating chromosome structure and promoting the assembly
of multicomponent protein
DNA complexes.
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