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J Bacteriol, May 1998, p. 2694-2700, Vol. 180, No. 10
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

In Vitro and In Vivo Oxidation of Methionine Residues in Small, Acid-Soluble Spore Proteins from Bacillus Species

Christopher S. Hayes, Berenice Illades-Aguiar,dagger Lilliam Casillas-Martinez, and Peter Setlow*

Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030

Received 29 December 1997/Accepted 16 March 1998

Methionine residues in alpha /beta -type small, acid-soluble spore proteins (SASP) of Bacillus species were readily oxidized to methionine sulfoxide in vitro by t-butyl hydroperoxide (tBHP) or hydrogen peroxide (H2O2). These oxidized alpha /beta -type SASP no longer bound to DNA effectively, but DNA binding protected alpha /beta -type SASP against methionine oxidation by peroxides in vitro. Incubation of an oxidized alpha /beta -type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce methionine sulfoxide residues back to methionine, restored the alpha /beta -type SASP's ability to bind to DNA. Both tBHP and H2O2 caused some oxidation of the two methionine residues of an alpha /beta -type SASP (SspC) in spores of Bacillus subtilis, although one methionine which is highly conserved in alpha /beta -type SASP was only oxidized to a small degree. However, much more methionine sulfoxide was generated by peroxide treatment of spores carrying a mutant form of SspC which has a lower affinity for DNA. MsrA activity was present in wild-type B. subtilis spores. However, msrA mutant spores were no more sensitive to H2O2 than were wild-type spores. The major mechanism operating for dealing with oxidative damage to alpha /beta -type SASP in spores is DNA binding, which protects the protein's methionine residues from oxidation both in vitro and in vivo. This may be important in vivo since alpha /beta -type SASP containing oxidized methionine residues no longer bind DNA well and alpha /beta -type SASP-DNA binding is essential for long-term spore survival.

* Corresponding author. Mailing address: Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06030. Phone: (860) 679-2607. Fax: (860) 679-3408. E-mail: setlow{at}sun.uchc.edu.

dagger Present address: Escuela de Ciencias Quimico Biologicas, Universidad Autonoma de Guerrero, Chilpancingo, Guerrero 39000, Mexico.

J Bacteriol, May 1998, p. 2694-2700, Vol. 180, No. 10
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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