Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the Archaebacterium, Sulfolobus solfataricus

Choli, Theodora; Henning, Petra; Wittmann‐Liebold, Brigitte; Reinhardt, Richard

doi:10.1016/0167-4781(88)90011-5

Cited by 82 publications

(83 citation statements)

References 27 publications

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“…We noticed that another chromatin protein, Sul7d, was methylated in vivo most intensively near its tails (Lys-5 and -7 and Lys-61, -63, and -64) by MS/MS assays (Table 1), which is in agreement with previous reports (19,23,24). Meanwhile, Lys-53 and Lys-49 were also detected to be methylated in native Sul7d, although to a relatively lower extent (Table 1), which is probably due to strain difference and variegated methylation pattern in Sulfolobus.…”

Section: Csl4-exosome and Rrp4-exosome Lanes)supporting

confidence: 82%

“…aKMT4 Possesses Intrinsic MTase Activity under Various Conditions-Because Sul7d constitutes the main scaffold of chromatin and has been shown to be methylated across Sulfolobus species (19,23,24), the recombinant protein expressed in E. coli was used as a prospective substrate to directly test if aKMT4 has intrinsic MTase activity. Increased covalent 3 H-methyl-Sul7d products were clearly visualized by autoradiography on the PVDF membrane after separation by SDS-PAGE when recombinant aKMT4 was incubated with the increasing amounts of substrate and […”

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

“…Among archaeal chromatin proteins, members of the Sul7d family are the most abundant, comprising about 5% of the soluble cellular proteins (19,23). Sul7d proteins are modified by monomethylation of N-or C-terminal lysine residues to different extents in a strain-dependent manner (23,24).…”

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confidence: 99%

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A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

Niu

Xia

Wang

et al. 2013

Journal of Biological Chemistry

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Background:The origin of eukaryotic histone modification enzymes still remains obscure. Results: Prototypic KMT4/Dot1 from Archaea targets chromatin proteins (Sul7d and Cren7) and shows increased activity on Sul7d, but not Cren7, in the presence of DNA. Conclusion: Promiscuous aKMT4 could be regulated by chromatin environment. Significance: This study supports the prokaryotic origin model of eukaryotic histone methyltransferases and sheds light on chromatin dynamics in Archaea.

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Section: Csl4-exosome and Rrp4-exosome Lanes)supporting

confidence: 82%

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

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A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

Niu

Xia

Wang

et al. 2013

Journal of Biological Chemistry

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“…Particularly, P2 was identical to the protein previously found in S. solfataricus and referred to as SsoTd [7], except for the replacement of Glu ~3 by Gin 13, and the lack of one lysine at the C-terminus. Subsequently, we cloned and overexpressed this protein in Escherichia coli [8].…”

Section: Introductionsupporting

confidence: 63%

“…isolated from S. acidocaldarius and S. solfataricus, and identified as DNA-binding proteins on the basis of their capacity to bind DNA aspecifically [5][6][7]. Particularly, P2 was identical to the protein previously found in S. solfataricus and referred to as SsoTd [7], except for the replacement of Glu ~3 by Gin 13, and the lack of one lysine at the C-terminus.…”

Section: Introductionmentioning

confidence: 85%

¹H‐NMR and photo‐CIDNP spectroscopies show a possible role for Trp²³ and Phe³¹ in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus

Consonni¹,

Limiroli

Molinari

et al. 1995

FEBS Letters

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Structural and dynamic effects of α‐Helix deletion in Sso7d: Implications for protein thermal stability

2004

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Sso7d is a 62-residue protein from the hyperthemophilic archaeon Sulfolobus solfataricus with a denaturation temperature close to 100 degrees C around neutral pH. An engineered form of Sso7d truncated at leucine 54 (L54Delta) is significantly less stable, with a denaturation temperature of 53 degrees C. Molecular dynamics (MD) studies of Sso7d and its truncated form at two different temperatures have been performed. The results of the MD simulations at 300 K indicate that: (1) the flexibility of Sso7d chain at 300 K agrees with that detected from X-ray and NMR structural studies; (2) L54Delta remains stable in the native folded conformation and possesses an overall dynamic behavior similar to that of the parent protein. MD simulations performed at 500 K, 10 ns long, indicate that, while Sso7d is in-silico resistant to high temperature, the truncated variant partially unfolds, revealing the early phases of the thermal unfolding pathway of the protein. Analysis of the trajectories of L54Delta suggests that the unzipping of the N-terminal and C-terminal beta-strands should be the first event of the unfolding pathway, and points out the regions more resistant to thermal unfolding. These findings allow one to understand the role played by specific interactions connecting the two ends of the chain for the high thermal stability of Sso7d, and support recent hypotheses on its folding mechanism emerged from site-directed mutagenesis studies.

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Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the Archaebacterium, Sulfolobus solfataricus

Cited by 82 publications

References 27 publications

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

¹H‐NMR and photo‐CIDNP spectroscopies show a possible role for Trp²³ and Phe³¹ in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus

Structural and dynamic effects of α‐Helix deletion in Sso7d: Implications for protein thermal stability

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Isolation, characterization and microsequence analysis of a small basic methylated DNA-binding protein from the Archaebacterium, Sulfolobus solfataricus

Cited by 82 publications

References 27 publications

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

1H‐NMR and photo‐CIDNP spectroscopies show a possible role for Trp23 and Phe31 in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus

Structural and dynamic effects of α‐Helix deletion in Sso7d: Implications for protein thermal stability

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¹H‐NMR and photo‐CIDNP spectroscopies show a possible role for Trp²³ and Phe³¹ in nucleic acid binding by P2 ribonuclease from the archaeon Sulfolobus solfataricus