ArticleThe Biochemical journal2010
Dimer-dimer stacking interactions are important for nucleic acid binding by the archaeal chromatin protein Alba.
Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Genome-wide analysis of the Alba gene family members in soybean (Glycine max L.): characterization and stress-responsive expression patterns.BMC plant biology · 2025Article
- Evolution of sequence, structural and functional diversity of the ubiquitous DNA/RNA-binding Alba domain.Scientific reports · 2024Article
- Dual dimeric interactions in the nucleic acid-binding protein Sac10b lead to multiple bridging of double-stranded DNA.Heliyon · 2024Article
- Genome-wide identification and expression profiling of Alba gene family members in response to abiotic stress in tomato (Solanum lycopersicum L.).BMC plant biology · 2021Article
- Archaea: The Final Frontier of Chromatin.Journal of molecular biology · 2021Review
- The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone.Nucleic acids research · 2020Article
- Structure and function of archaeal histones.PLoS genetics · 2018Review
- Transcription Regulation in Archaea.Journal of bacteriology · 2016Review
- The PfAlba1 RNA-binding protein is an important regulator of translational timing in Plasmodium falciparum blood stages.Genome biology · 2015Article
- Chromatin structure and dynamics in hot environments: architectural proteins and DNA topoisomerases of thermophilic archaea.International journal of molecular sciences · 2014Review
- Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea.The Journal of biological chemistry · 2014Article
- Article
- PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites.Nucleic acids research · 2012Article
- Crystal structure of archaeal chromatin protein Alba2-double-stranded DNA complex from Aeropyrum pernix K1.The Journal of biological chemistry · 2012Article
- Alba shapes the archaeal genome using a delicate balance of bridging and stiffening the DNA.Nature communications · 2012Article
- Molecular mechanism underlying the interaction of typical Sac10b family proteins with DNA.PloS one · 2012Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Archaea use a variety of small basic proteins to package their DNA. One of the most widespread and highly conserved is the Alba (Sso10b) protein. Alba interacts with both DNA and RNA in vitro, and we show in the present study that it binds more tightly to dsDNA (double-stranded DNA) than to either ssDNA (single-stranded DNA) or RNA. The Alba protein is dimeric in solution, and forms distinct ordered complexes with DNA that have been visualized by electron microscopy studies; these studies suggest that, on binding dsDNA, the protein forms extended helical protein fibres. An end-to-end association of consecutive Alba dimers is suggested by the presence of a dimer-dimer interface in crystal structures of Alba from several species, and by the strong conservation of the interface residues, centred on Arg59 and Phe60. In the present study we map perturbation of the polypeptide backbone of Alba upon binding to DNA and RNA by NMR, and demonstrate the central role of Phe60 in forming the dimer-dimer interface. Site-directed spin labelling and pulsed ESR are used to confirm that an end-to-end, dimer-dimer interaction forms in the presence of dsDNA.
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Registered trials
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