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Journal of Bacteriology, April 2000, p. 1942-1948, Vol. 182, No. 7
Department of Biochemistry, University of
Connecticut Health Center, Farmington, Connecticut 06032
Received 1 October 1999/Accepted 17 December 1999
HBsu, the Bacillus subtilis homolog of the
Escherichia coli HU proteins and the major chromosomal
protein in vegetative cells of B. subtilis, is present at
similar levels in vegetative cells and spores (~5 × 104 monomers/genome). The level of HBsu in spores was
unaffected by the presence or absence of the
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Copyright © 2000, American Society for Microbiology. All rights reserved.
The Bacillus subtilis HBsu Protein Modifies the
Effects of
/
-Type, Small Acid-Soluble Spore Proteins on
DNA
/
-type, small
acid-soluble proteins (SASP), which are the major chromosomal proteins
in spores. In developing forespores, HBsu colocalized with
/
-type
SASP on the nucleoid, suggesting that HBsu could modulate
/
-type SASP-mediated properties of spore DNA. Indeed, in vitro studies showed
that HBsu altered
/
-type SASP protection of pUC19 from DNase
digestion, induced negative DNA supercoiling opposing
/
-type SASP-mediated positive supercoiling, and greatly ameliorated the
/
-type SASP-mediated increase in DNA persistence length. However, HBsu did not significantly interfere with the
/
-type
SASP-mediated changes in the UV photochemistry of DNA that explain the
heightened resistance of spores to UV radiation. These data strongly
support a role for HBsu in modulating the effects of
/
-type SASP
on the properties of DNA in the developing and dormant spore.
*
Corresponding author. Mailing address: Department of
Biochemistry, University of Connecticut Health Center, Farmington, CT 06032. Phone: (860) 679-2607. Fax: (860) 679-3408. E-mail:
setlow{at}sun.uchc.edu.
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