Journal
STRUCTURE
Volume 13, Issue 7, Pages 963-971Publisher
CELL PRESS
DOI: 10.1016/j.str.2005.04.016
Keywords
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Funding
- Biotechnology and Biological Sciences Research Council [C18024] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [C18024] Funding Source: researchfish
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Organisms growing at elevated temperatures face a particular challenge to maintain the integrity of their genetic material. All thermophilic and hyperthermophilic archaea encode one or more copies of the Alba (Sac10b) gene. Alba is an abundant, dimeric, highly basic protein that binds cooperatively and at high density to DNA. Sulfolobus solfataricus encodes a second copy of the Alba gene, and the Alba2 protein is expressed at 5% of the level of Alba1. We demonstrate by NMR, ITC, and crystallography that Alba2 exists exclusively as a heterodimer with Alba1 at physiological concentrations and that heterodimerization exerts a clear effect upon the DNA packaging, as observed by EM, potentially by changing the interface between adjacent Alba dimers in DNA complexes. A functional role for Alba2 in modulation, of higher order chromatin structure and DNA condensation is suggested.
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