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Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species.

ABSTRACT: The DNA-binding alpha/beta-type small acid-soluble proteins (SASPs) are a major factor in the resistance and long-term survival of spores of Bacillus species by protecting spore DNA against damage due to desiccation, heat, toxic chemicals, enzymes, and UV radiation. We now report the crystal structure at 2.1 A resolution of an alpha/beta-type SASP bound to a 10-bp DNA duplex. In the complex, the alpha/beta-type SASP adopt a helix-turn-helix motif, interact with DNA through minor groove contacts, bind to approximately 6 bp of DNA as a dimer, and the DNA is in an A-B type conformation. The structure of the complex provides important insights into the molecular details of both DNA and alpha/beta-type SASP protection in the complex and thus also in spores.

SUBMITTER: Lee KS

PROVIDER: S-EPMC2268541 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature

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Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species.

Lee Ki Seog KS Bumbaca Daniela D Kosman Jeffrey J Setlow Peter P Jedrzejas Mark J MJ

Proceedings of the National Academy of Sciences of the United States of America 20080219 8

The DNA-binding alpha/beta-type small acid-soluble proteins (SASPs) are a major factor in the resistance and long-term survival of spores of Bacillus species by protecting spore DNA against damage due to desiccation, heat, toxic chemicals, enzymes, and UV radiation. We now report the crystal structure at 2.1 A resolution of an alpha/beta-type SASP bound to a 10-bp DNA duplex. In the complex, the alpha/beta-type SASP adopt a helix-turn-helix motif, interact with DNA through minor groove contacts, ...[more]

PMID: 18287075

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