Work

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

Year: 2008

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.0708244105

Authors: Ki Seog Lee, Daniela Bumbaca, Jeffrey Kosman, Peter Setlow, Mark J. Jedrzejas

Institution: UConn Health

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: DEGRADATION REACTIONS IN SPORE GERMINATION, G3347162900, Degradation Reactions in Spore Germination