Deletion of the archaeal histone in <i>Methanosarcina mazei</i> Gö1 results in reduced growth and genomic transcription

Weidenbach, Katrin; Glöer, Jens; Ehlers, Claudia; Sandman, Kathleen; Reeve, John N.; Schmitz, Ruth A.

doi:10.1111/j.1365-2958.2007.06076.x

Cited by 43 publications

(39 citation statements)

References 55 publications

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“…However, the abundance of a variety of cellular proteins from the four mutants varied, indicating a pleiotropic effect on gene expression. The requirement for an archaeal histone was then evaluated in Methanosarcina mazei Göl by insertional disruption of the only histone, HMm [21]. Loss of HMm was not lethal but resulted in mutants that have impaired ability to grow on methanol and trimethylamine, suggesting that the archaeal histone is dispensible.…”

Section: Archaeal Histonesmentioning

confidence: 99%

Archaeal chromatin proteins

Zhang

Guo

Huang

2012

Sci. China Life Sci.

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Archaea, along with Bacteria and Eukarya, are the three domains of life. In all living cells, chromatin proteins serve a crucial role in maintaining the integrity of the structure and function of the genome. An array of small, abundant and basic DNA-binding proteins, considered candidates for chromatin proteins, has been isolated from the Euryarchaeota and the Crenarchaeota, the two major phyla in Archaea. While most euryarchaea encode proteins resembling eukaryotic histones, crenarchaea appear to synthesize a number of unique DNA-binding proteins likely involved in chromosomal organization. Several of these proteins (e.g., archaeal histones, Sac10b homologs, Sul7d, Cren7, CC1, etc.) have been extensively studied. However, whether they are chromatin proteins and how they function in vivo remain to be fully understood. Future investigation of archaeal chromatin proteins will lead to a better understanding of chromosomal organization and gene expression in Archaea and provide valuable information on the evolution of DNA packaging in cellular life.Archaea, chromatin protein, biochemical properties, structure, post-translational modification Citation:

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Section: Archaeal Histonesmentioning

confidence: 99%

Archaeal chromatin proteins

Zhang

Guo

Huang

2012

Sci. China Life Sci.

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“…Inactivation of the single histone-encoding gene in Methanosarcina mazei was possible, but the resulting strain exhibited reduced growth, UV sensitivity, and global transcriptome changes (41). Similarly, inactivation of either of the two histone-encoding genes in the distantly related methanogen Methanococcus voltae was not lethal, but the resulting strains had proteome differences (10).…”

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confidence: 99%

An Archaeal Histone Is Required for Transformation of Thermococcus kodakarensis

et al. 2012

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dArchaeal histones wrap DNA into complexes, designated archaeal nucleosomes, that resemble the tetrasome core of a eukaryotic nucleosome. Therefore, all DNA interactions in vivo in Thermococcus kodakarensis, the most genetically versatile model species for archaeal research, must occur in the context of a histone-bound genome. Here we report the construction and properties of T. kodakarensis strains that have TK1413 or TK2289 deleted, the genes that encode HTkA and HTkB, respectively, the two archaeal histones present in this archaeon. All attempts to generate a strain with both TK1413 and TK2289 deleted were unsuccessful, arguing that a histone-mediated event(s) in T. kodakarensis is essential. The HTkA and HTkB amino acid sequences are 84% identical (56 of 67 residues) and 94% similar (63 of 67 residues), but despite this homology and their apparent redundancy in terms of supporting viability, the absence of HTkA and HTkB resulted in differences in growth and in quantitative and qualitative differences in genome transcription. A most surprising result was that the deletion of TK1413 (⌬htkA) resulted in a T. kodakarensis strain that was no longer amenable to transformation, whereas the deletion of TK2289 (⌬htkB) had no detrimental effects on transformation. Potential roles for the archaeal histones in regulating gene expression and for HTkA in DNA uptake and recombination are discussed.T he histone fold apparently evolved before the archaeal and eukaryotic lineages diverged ϳ1.5 to 1.9 billion years ago, and now almost all eukaryotes, Euryarchaea, Nanoarchaea, Thaumarchaea, and some Crenarchaea employ histone fold-based DNA binding to wrap and compact their genomic DNA (2,9,14,21,28,30,38). All transactions in these species that involve chromosomal DNA must therefore be considered in terms of histone-bound chromatin. The presence of histones in Archaea, but not in Bacteria, was a major distinction first recognized ϳ20 years ago (26), and research since then has established the detailed structure of archaeal histones (3, 19); the composition and architecture of the archaeal nucleosome (11,20,22,24,30); and the consequences of archaeal histone binding on DNA topology, replication, and transcription in vitro (7,37,43,44). Archaeal nucleosomes resemble the eukaryotic tetrasome, the structure at the center of the eukaryotic nucleosome formed by ϳ90 bp of DNA wrapped around a histone (H3ϩH4) 2 tetramer (20,28,30). Archaeal histones do not, however, have homologues of the N-and C-terminal amino acid extensions (21) that contain the targets for eukaryotic histone acetylation and methylation and thus provide the basis for epigenetic regulation. Consistent with this, scrutiny of archaeal genome sequences has failed to detect recognizable homologues of the eukaryotic histone modification systems, and to date, no archaeal histone modification has been described (5). It is therefore intriguing and important to determine if archaeal histones nevertheless participate in regulating genome functions. In this regard, in species ...

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“…They are present in all archaeons except Halobacteria and Methanomicrobia (Euryarchaea). For instance, Methanosarcina sequenced genomes contain one gene coding for a true archaeal histone, HMm, as well as genes coding for structural proteins of the methanogen chromosomal protein 1 (MC1) family [8].…”

Section: Introductionmentioning

confidence: 99%

Refined solution structure and backbone dynamics of the archaeal MC1 protein

et al. 2010

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The 3D structure of methanogen chromosomal protein 1 (MC1), determined with heteronuclear NMR methods, agrees with its function in terms of the shape and nature of the binding surface, whereas the 3D structure determined with homonuclear NMR does not. The structure features five loops, which show a large distribution in the ensemble of 3D structures. Evidence for the fact that this distribution signifies internal mobility on the nanosecond time scale was provided by using 15N‐relaxation and molecular dynamics simulations. Structural variations of the arm (11 residues) induced large shape anisotropy variations on the nanosecond time scale that ruled out the use of the model‐free formalism to analyze the relaxation data. The backbone dynamics analysis of MC1 was achieved by comparison with 20 ns molecular dynamics trajectories. Two β‐bulges showed that hydrogen bond formation correlated with ϕ and ψ dihedral angle transitions. These jumps were observed on the nanosecond time scale, in agreement with a large decrease in 15N‐NOE for Gly17 and Ile89. One water molecule bridging NH(Glu87) and CO(Val57) through hydrogen bonding contributed to these dynamics. Nanosecond slow motions observed in loops LP3 (35–42) and LP5 (67–77) reflected the lack of stable hydrogen bonds, whereas the other loops, LP1 (10–14), LP2 (22–24), and LP4 (50–53), were stabilized by several hydrogen bonds. Dynamics are often directly related to function. Our data strongly suggest that residues belonging to the flexible regions of MC1 could be involved in the interaction with DNA.

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Deletion of the archaeal histone in Methanosarcina mazei Gö1 results in reduced growth and genomic transcription

Cited by 43 publications

References 55 publications

Archaeal chromatin proteins

Archaeal chromatin proteins

An Archaeal Histone Is Required for Transformation of Thermococcus kodakarensis

Refined solution structure and backbone dynamics of the archaeal MC1 protein

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