Electron microscopic study of DNA complexes with proteins from the Archaebacterium <i>Sulfolobus acidocaldarius</i>

Grote, Mathias; Dijk, Jan; Reinhardt, Richard; Dobrinski, Beate

doi:10.1002/j.1460-2075.1986.tb04705.x

Cited by 92 publications

(144 citation statements)

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“…The protein eluting around fractions 36 to 40 was identified by mass spectrometry as the T. tenax Alba (Sac10b) ortholog. Alba is known to interact with single-stranded DNA, double-stranded DNA, and RNA (10,14,15). The TtxAlba protein was purified to homogeneity by gel filtration chromatography prior to all further characterization.…”

Section: Resultsmentioning

confidence: 99%

“…The bacterial chromatin proteins include HU, IHF, Fis, and H-NS, and there is variable distribution of these proteins across the bacterial family tree (25). The archaea have a different set of chromatin proteins, including a true histone protein, which organizes DNA into tetrameric nucleosomes (20), and the dimeric Alba protein, which can form extended filamentous fibers with DNA (12,14). The distribution of these proteins is complex, with the histones primarily restricted to the euryarchaea (with the notable exception of Cenarchaeum symbiosum, a marine crenarchaeote [7]) and Alba present in most archaea with the exception of the Methanosarcinales and halophiles.…”

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confidence: 99%

“…Purified chromatin proteins tend to form extended filaments when they are bound to DNA (14), and it has been suggested that expression of multiple chromatin proteins provides a mechanism for the control of this phenomenon in vivo (19). Notable exceptions to this rule are the genomes of Pyrobaculum aerophilum and Aeropyrum pernix, which have one and two copies of the Alba gene, respectively, but no other genes for known chromatin proteins (9).…”

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CC1, a Novel Crenarchaeal DNA Binding Protein

et al. 2007

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The genomes of the related crenarchaea Pyrobaculum aerophilum and Thermoproteus tenax lack any obvious gene encoding a single-stranded DNA binding protein (SSB). SSBs are essential for DNA replication, recombination, and repair and are found in all other genomes across the three domains of life. These two archaeal genomes also have only one identifiable gene encoding a chromatin protein (the Alba protein), while most other archaea have at least two different abundant chromatin proteins. We performed a biochemical screen for novel nucleic acid binding proteins present in cell extracts of T. tenax. An assay for proteins capable of binding to a single-stranded DNA oligonucleotide resulted in identification of three proteins. The first protein, Alba, has been shown previously to bind single-stranded DNA as well as duplex DNA. The two other proteins, which we designated CC1 (for crenarchaeal chromatin protein 1), are very closely related to one another, and homologs are restricted to the P. aerophilum and Aeropyrum pernix genomes. CC1 is a 6-kDa, monomeric, basic protein that is expressed at a high level in T. tenax. This protein binds single-and double-stranded DNAs with similar affinities. These properties are consistent with a role for CC1 as a crenarchaeal chromatin protein.

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Section: Resultsmentioning

confidence: 99%

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CC1, a Novel Crenarchaeal DNA Binding Protein

et al. 2007

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“…Most of Sac10b homologues with basic isoelectric points (for example: 10.5 for Sac10b and Ssh10b, 9.7 for Mja10b, 9.4 for Sso10b, 8.0 for Mth10b, and 7.9 for Mvo 10b) show cooperative and more or less strong DNA binding without apparent sequence specificity [27,42,44] (pIs were calculated from the amino acid compositions of the corresponding proteins). However, some mesophilic members of the Sac10b protein family have a slightly acidic pI.…”

Section: Biophysical and Biochemical Properties Of The Sac10b Proteinsmentioning

confidence: 99%

The Archaeal Sac10b Protein Family: Conserved Proteins with Divergent Functions

Xuan¹,

Feng²

2012

CPPS

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Abstract:Here we review the present state of structural and functional studies of the Sac10b protein family, a class of highly conserved 10 kDa nucleic acid-binding proteins in archaea. Based on biochemical and structural studies, these proteins were originally assigned a role in the structural organization of chromatin; Sac10b proteins of hyperthermophilic archaea, for example, showed tight, unspecific DNA binding. More recently, however, Sac10b proteins of mesophilic archaea were found to interact preferentially with specific DNA sequences thereby affecting the expression of distinct genes. Furthermore, Sac10b proteins of hyperthermophilic, thermophilic and mesophilic archaea were also shown to bind to RNA with distinct affinities and specificities but functional consequences of RNA binding of these proteins, besides perhaps RNA stabilization, have not yet been observed. To better understand the physiological meaning of the various interactions of Sac10b proteins with nucleic acids, future work should concentrate on elucidating the molecular structures of complexes of Sac10b proteins of hyperthermophilic and mesophilic archaea with DNA and RNA. In addition, existing and new X-ray and NMR structures of individual hyperthermophilic Sac10b proteins may represent very good models for introducing thermostability especially in enzymes for industrial use.

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“…These findings suggest that the archaebacterial chromosome resembles that of eucaryotes rather than that of most other procaryotes. However, it was recently shown that some DNA-binding proteins isolated from the acidothermophilic archaebacterium Sulfolobus acidocaldarius do not form the nucleosomelike structure but do form another type of structure (13). Thus, investigations showing the chromosomal structure directly are warranted.…”

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confidence: 99%