ArticleJournal of bacteriology2009
The Sac10b homolog in Methanococcus maripaludis binds DNA at specific sites.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Evolution of sequence, structural and functional diversity of the ubiquitous DNA/RNA-binding Alba domain.Scientific reports · 2024Article
- DNA-bridging by an archaeal histone variant via a unique tetramerisation interface.Communications biology · 2023Article
- Growth temperature and chromatinization in archaea.Nature microbiology · 2022Article
- Diversity of gut methanogens and functional enzymes associated with methane metabolism in smallholder dairy cattle.Archives of microbiology · 2022Article
- 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
- The Role of Archaeal Chromatin in Transcription.Journal of molecular biology · 2019Review
- The archaeal RNA chaperone TRAM0076 shapes the transcriptome and optimizes the growth of Methanococcus maripaludis.PLoS genetics · 2019Article
- Structure and function of archaeal histones.PLoS genetics · 2018Review
- TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA.PloS one · 2016Article
- The interplay between nucleoid organization and transcription in archaeal genomes.Nature reviews. Microbiology · 2015Review
- 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
- PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The Sac10b protein family, also known as Alba, is widely distributed in Archaea. Sac10b homologs in thermophilic Sulfolobus species are very abundant. They bind both DNA and RNA with high affinity and without sequence specificity, and their physiological functions are still not fully understood. Mma10b from the euryarchaeote Methanococcus maripaludis is a mesophilic member of the Sac10b family. Mma10b is not abundant and constitutes only approximately 0.01% of the total cellular protein. Disruption of mma10b resulted in poor growth of the mutant in minimal medium at near the optimal growth temperature but had no detectable effect on growth in rich medium. Quantitative proteomics, real time reverse transcription-PCR, and enzyme assays revealed that the expression levels of some genes involved in CO(2) assimilation and other activities were changed in the Deltamma10b mutant. Chromatin immunoprecipitation suggested a direct association of Mma10b with an 18-bp DNA binding motif in vivo. Electrophoretic mobility shift assays and DNase I footprinting confirmed that Mma10b preferentially binds specific sequences of DNA with an apparent Kd in the 100 nM range. These results suggested that the physiological role of Mma10b in the mesophilic methanococci is greatly diverged from that of homologs in thermophiles.
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Registered trials
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