Mutational analysis of genes encoding chromatin proteins in the archaeon Methanococcus voltae indicates their involvement in the regulation of gene expression

Heinicke, I.; Müller, Jan; Pittelkow, Marco; Klein, Albrecht

doi:10.1007/s00438-004-1033-5

Cited by 41 publications

(30 citation statements)

References 66 publications

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“…Mvo10b, for example, is a Sac10b chromatin protein from the mesophilic methanogenic archaeon Methanococcus voltae with an optimal growth temperature of ~37°C. Deletion of the mvo10b gene did not affect viability and growth of the mutant archaeon but changed the protein expression pattern relative to that of the wild-type as revealed by 2D gel electrophoresis of cell extracts [59]. Recently [60], we cloned and expressed recombinant Mvo10b in E. coli.…”

Section: Functional Divergence -Functions Of Sac10b Family Members Inmentioning

confidence: 99%

“…It is interesting that the expression levels of these proteins are positively correlated with methanococcal optimum growth temperatures. The fact that both Mma10b and Mvo10b constituted only ~0.01 % each of the total cellular protein suggested that these mesophilic proteins participated in the regulation of distinct genes but it cannot be excluded that they are also involved in the regulation of chromatin structure [42,59] and that the two functions overlap.…”

Section: Functional Divergence -Functions Of Sac10b Family Members Inmentioning

confidence: 99%

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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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Section: Functional Divergence -Functions Of Sac10b Family Members Inmentioning

confidence: 99%

Section: Functional Divergence -Functions Of Sac10b Family Members Inmentioning

confidence: 99%

The Archaeal Sac10b Protein Family: Conserved Proteins with Divergent Functions

Xuan¹,

Feng²

2012

CPPS

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“…A few homologs of eukaryal transcriptional regulators (33) and unique archaeal regulators (57) as well as non-sequencespecific DNA binding proteins (5,30) have been investigated for their contribution to the regulation of archaeal genes.…”

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confidence: 99%

MarR-Like Transcriptional Regulator Involved in Detoxification of Aromatic Compounds in Sulfolobus solfataricus

et al. 2007

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A DNA binding protein, BldR, was identified in the crenarchaeon Sulfolobus solfataricus as a protein 5-to 10-fold more abundant in cells grown in the presence of toxic aldehydes; it binds to regulatory sequences located upstream of an alcohol dehydrogenase gene (Sso2536). BldR is homologous to bacterial representatives of the MarR (multiple antibiotic resistance) family of transcriptional regulators that mediate response to multiple environmental stresses. Transcriptional analysis revealed that the bldR gene was transcribed in a bicistronic unit composed of the genes encoding the transcriptional regulator (Sso1352) and a putative multidrug transporter (Sso1351) upstream. By homology to bacterial counterparts, the bicistron was named the mar-like operon. The level of mar-like operon expression was found to be increased at least 10-fold in response to chemical stress by aromatic aldehydes. Under the same growth conditions, similar enhanced in vivo levels of Sso2536 gene transcript were also measured. The gene encoding BldR was expressed in E. coli, and the recombinant protein was purified to homogeneity. DNA binding assays demonstrated that the protein is indeed a transcription factor able to recognize site specifically both the Sso2536 and mar-like promoters at sites containing palindromic consensus sequences. Benzaldehyde, the substrate of ADH Ss , stimulates DNA binding of BldR at both promoters. The role of BldR in the auto-activation as well as in the regulation of the Sso2536 gene, together with results of increased operon and gene expression under conditions of exposure to aromatic aldehydes, indicates a novel coordinate regulatory mechanism in cell defense against stress by aromatic compounds.A chimeric nature of the transcription machinery with eukaryote-like basal factors and bacterium-like regulative components has been found in all members of the domain Archaea (50, 60). In fact, in most cases, homologs of bacterial regulators function in the context of the archaeal basal transcriptional apparatus, which resembles that of Eukarya (8, 26). Transcription initiation is mediated by a single RNA polymerase (RNAP) and two general transcription factors, TATA element binding protein (TBP) and transcription factor B (TFB), a homologue of the transcription factor TFIIB, which binds to the B recognition element (BRE) and determines the directionality of the transcription (7). The complex containing RNAP, TBP, and TFB is sufficient to initiate transcription in cell-free systems (31, 49), although an additional factor, transcription factor E, is required to increase transcription from some promoters (6, 29).A few homologs of eukaryal transcriptional regulators (33) and unique archaeal regulators (57) as well as non-sequencespecific DNA binding proteins (5, 30) have been investigated for their contribution to the regulation of archaeal genes.Homologs of bacterial transcriptional regulators are more common in Archaea, and representatives that have been studied experimentally include the Lrp homologs (13) that can fun...

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“…The number of peptide pairs collected per ORF was designated n. The relative signal intensity (peak height) of 14 N and 15 N peptide peaks in each peak pair was used as a measure of relative peptide level. Multiple measurements of one protein were averaged to obtain the relative protein levels in S2 and S590.…”

Section: Methodsmentioning

confidence: 99%

“…In addition, the readily available genetic systems in mesophilic methanococci are of value for the investigation of the in vivo role of the Sac10b family. Heinicke et al (14) constructed a mutant of the mesophilic, heterotrophic Methanococcus voltae with a deletion of the gene encoding a Sac10b homolog. While the mutation did not affect growth in complex medium, two-dimensional gel electrophoresis of the cellular proteins identified changes in the expression of genes encoding a helix-turn-helix DNA binding protein, a cystathione ␤-synthase domain-containing protein, and pyruvate oxidoreductase (Por) subunit C (14).…”

mentioning

confidence: 99%

The Sac10b Homolog in Methanococcus maripaludis Binds DNA at Specific Sites

Liu¹,

Guo

et al. 2009

J Bacteriol

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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 ϳ0.01% 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 ⌬mma10b 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 K d 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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Mutational analysis of genes encoding chromatin proteins in the archaeon Methanococcus voltae indicates their involvement in the regulation of gene expression

Cited by 41 publications

References 66 publications

The Archaeal Sac10b Protein Family: Conserved Proteins with Divergent Functions

The Archaeal Sac10b Protein Family: Conserved Proteins with Divergent Functions

MarR-Like Transcriptional Regulator Involved in Detoxification of Aromatic Compounds in Sulfolobus solfataricus

The Sac10b Homolog in Methanococcus maripaludis Binds DNA at Specific Sites

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