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PubMed2002

Systemic lupus erythematosus and related autoimmune diseases are antigen-driven, epigenetic diseases.

Autoimmune diseases result when cellular stresses (ex UV, cell cycle, hormones, viruses, and/or drugs) induce altered expression of polyamines, leading to chromatin disruption, interference with chromatin methylation, exposure of sequestered genes, and interference with tissue-specific processes. Exposure of previously sequestered Alu and LINE-1 sequences can lead to reverse transcription of Alu-RNA (and other transcripts) by the LINE-1 reverse transcriptase, yielding autoantigenic, hypomethylated DNA fragments. Release from the cell of the hypomethylated DNA fragments, along with polyamine-associated nucleoprotein complexes formed with the fragments, would elicit the autoimmune response. Loss of gene control due to hypomethylation and chromatin disruption by polyamines or other factors can include loss of dosage compensation from the inactive X chromosome for spermine synthase and spermidine/spermine N(1)-acetyltransferase at Xp22.1. This leads to ongoing altered polyamine levels. Thus, autoimmune diseases result from epigenetic changes that lead to autoantigen generation.

Autoantigens↗

PubMed2003

F factor conjugation is a true type IV secretion system.

The F sex factor of Escherichia coli is a paradigm for bacterial conjugation and its transfer (tra) region represents a subset of the type IV secretion system (T4SS) family. The F tra region encodes eight of the 10 highly conserved (core) gene products of T4SS including TraAF (pilin), the TraBF, -KF (secretin-like), -VF (lipoprotein) and TraCF (NTPase), -EF, -LF and TraGF (N-terminal region) which correspond to TrbCP, -IP, -GP, -HP, -EP, -JP, DP and TrbLP, respectively, of the P-type T4SS exemplified by the IncP plasmid RP4. F lacks homologs of TrbBP (NTPase) and TrbFP but contains a cluster of genes encoding proteins essential for F conjugation (TraFF, -HF, -UF, -WF, the C-terminal region of TraGF, and TrbCF) that are hallmarks of F-like T4SS. These extra genes have been implicated in phenotypes that are characteristic of F-like systems including pilus retraction and mating pair stabilization. F-like T4SS systems have been found on many conjugative plasmids and in genetic islands on bacterial chromosomes. Although few systems have been studied in detail, F-like T4SS appear to be involved in the transfer of DNA only whereas P- and I-type systems appear to transport protein or nucleoprotein complexes. This review examines the similarities and differences among the T4SS, especially F- and P-like systems, and summarizes the properties of the F transfer region gene products.

Amino Acid Sequence↗

PubMed2002

The in vivo function of phage phi29 nucleoid-associated protein p6 requires formation of dimers.

The Bacillus subtilis phage phi29 nucleoid-associated protein p6 (103 amino acids) is essential for in vivo viral DNA replication and control of transcription, and it has been proposed to play a role in genome organization and compaction. This protein self-associates in vitro from preformed dimers forming high-molecular-weight oligomers and binds to double-stranded DNA giving rise to multimeric nucleoprotein complexes. Site-directed mutants, p6I8T and p6A44V, were completely or partially inactive, respectively, in an in vitro dimerization assay. In this paper, and by in vivo crosslinking, we have detected dimers of protein p6 either in phage-infected cells or in protein p6 producing B. subtilis or Escherichia coli cells. Therefore, this self-association does not require viral DNA. We also show that mutants p6I8T and p6A44V are deficient in dimer formation, and they do not support phage DNA replication in a trans-complementation assay with phi29sus6 mutant-infected B. subtilis cells. We conclude that dimeric protein p6 is the active form of the protein in vivo, required for viral DNA replication.

Bacillus Phages↗

PubMed1997

The cardiac-muscle specific enhancer-promoter of slow/cardiac troponin C binds HMG-2.

The cardiac muscle-specific enhancer-promoter of the slow/cardiac troponin C (cTnC) gene contains five protein binding regions, four of which bind cardiac-myocyte specific proteins. We screened a stage 11 chick embryo expression library with a double-stranded oligonucleotide probe consisting of one of these regions, CEF-1. One of the clones obtained was the chicken high mobility group protein, HMG-2. An electrophoretic gel mobility shift assay (EMSA) showed a specific binding interaction between the HMG-2 protein and the dsDNA CEF-1 probe. The cardiac-specific enhancer region of cTnC contains at least one possible HMG binding region and it is in the CEF-1 sequence overlapping a known GATA-4 binding site. Mutation of the nucleotide sequence of this HMG binding region diminishes its protein binding ability and markedly decreases its cardiac specific transcriptional activity. HMG-2 is a DNA bending protein that is predominantly found in the nucleus in proliferating cells and in the cytoplasm of terminally differentiated cells. It is an integral and stabilizing factor in the transcription activation nucleoprotein complex and is often described as an 'architectural transcription factor'. It markedly stimulates the transcription of many genes, often in association with tissue-specific transcription factors. We believe that the presence of HMG-2 in the enhancer-promoter binding protein complex of cTnC augments DNA bending and facilitates the DNA binding and interaction of other tissue-specific factors (e.g. GATA-4, which also binds to this region). This would result in increased transcription of the cTnC gene during the proliferation phase of embryonic cardiac myocyte development.

Animals↗

PubMed1998

Characterization of an element positively regulating the transcription of MSSP gene-2 which encodes C-MYC binding proteins.

MSSP gene-2 encodes at least three alternative splicing products, MSSP-1, MSSP-2, and Scr2, which have been implied to function as factors regulating DNA replication, transcription, apoptosis induction, and cell-cycle movement, via the interaction with C-MYC. We have previously shown that the Mup1 sequence from -474 to -440 in the region required for transactivation of the MSSP gene-2 was protected from DNaseI digestion in vitro. Here, we report that the Mup1 sequence carries a positive transcriptional activity, and that the activity was lost by point mutations that inhibited the formation of specific nucleoprotein complexes on the sequence. In Southwestern analyses, two proteins of 38 and 62kDa directly interacted with the Mup1 sequence.

Alternative Splicing↗

PubMed1998

Regulatory implications of protein assemblies at the gamma origin of plasmid R6K - a review.

Recognition of the replication origin (ori) by initiator protein is a recurring theme for the regulated initiation of DNA replication in diverse biological systems. The objective of the work reviewed here is to understand the initiation process focusing specifically on the gamma-ori of the antibiotic-resistance plasmid R6K. The control of gamma-ori copy number is determined by both plasmid-encoded and host-encoded factors. The two central regulatory elements of the plasmid are a multifunctional initiator protein pi, and sequence-related DNA target sites, the inverted half-repeats (IRs) and the direct repeats (DRs). The replication activator and inhibitor activities of pi seem to be at least partially distributed between two naturally occurring pi polypeptides (designated by their molecular weights pi35.0 and pi30.5). Regulatory variants of pi with altered states of oligomerization in nucleoprotein complexes with DRs and IRs have been isolated. The properties of these mutants laid the foundation for our model of pi protein activity which proposes that different protein surfaces are required for the formation of functionally distinct complexes of pi with DRs and IRs. These mutants also suggest that pi polypeptides have a modular structure; the C-terminus contains the DNA-binding domain while the N-terminus controls protein oligomerization. Additionally, pi35.0 binds to a novel DNA sequence in the A+T-rich segment of gamma-ori. This binding site is at or near the site from which synthesis of the leading strand begins.

Base Sequence↗

PubMed1999

Structure of genes encoding chromosomal HMG1 proteins from maize.

The high mobility group (HMG) proteins of the HMG1 family are architectural proteins in chromatin that are considered to facilitate the formation of complex nucleoprotein structures in various biological processes such as transcription and recombination. Plants express a variety of these non-sequence-specific DNA-bending proteins. The sequences encoding the maize HMGa and HMGc1 proteins were isolated from a genomic DNA library. Determination of the nucleotide sequences of these genes revealed that the coding region of both genes has a similar genomic structure, comprising seven exons and six introns. The positioning of the introns is conserved between the two genes, whereas the number of introns and their positions are entirely different in the related animal genes. In the 5' flanking region of the hmgc1 gene, a copia-like retrotransposon was identified. In addition to the genes encoding HMGa and HMGc1, several genomic fragments (retropseudo gene, fragments of the genes) were isolated and characterised.

Amino Acid Sequence↗

PubMed1997

Cell specific nuclear antigens of boar spermatozoa.

Demembranated boar sperm heads were differentially extracted at conditions involving high salt-urea, proteolysis and DNase I cleavage that mimic the conditions promoting the in vivo decondensation of the fertilizing sperm nucleus in the egg ooplasm. The sperm-unique subset of proteins was studied which remained bound in the residual salt-resistant nuclear structure operationally defined as sperm nuclear matrix. By means of polyvalent antisera the immune specificity of the sperm nucleoprotein complex was estimated using ELISA and microcomplement fixation test as compared to somatic type dehistonized chromatin of boar liver. To define immunologically specific sperm DNA-associated proteins hybridomas were generated by fusing lymphocytes immunized with boar sperm protein/DNA complex. Monoclonal antibodies were selected (Mab 1A8, 1B3, 2B5, 2H5 and 3A4) which identified protein moieties in the sperm DNA-tight binding proteins complex resistant to cleavage with DNase I and sensitive upon digestion with high concentration of proteases. No appreciable reactivity was recorded of the antibodies to somatic chromatin and no significant binding to ssDNA. A polypeptide in the residual sperm nuclear structure of apparent Mr 27 kDa was recognized by Mab 3A4 as detected by Western blotting. The enhanced reactivity to the DNase I digested sperm nuclear fraction (except for Mab 2H5) suggests that DNA protected from nuclease digestion by a protein might be essential for immune reactivity and full antigenic integrity as well as the dependence of the cognate proteins on the binding to DNA for antigenicity and immune specificity. The functioning of the identified putative sperm specific proteins is anticipated in the structural rearrangement of chromatin in the zygote.

Animals↗

PubMed1996

Regulation of gene expression at early stages of B-cell and T-cell differentiation.

The expression of distinct sets of genes at different stages of B-lymphocyte and T-lymphocyte differentiation is controlled at the level of transcription. A number of recent studies have described interactions between transcription factors in lymphocytes that provide new insights into mechanisms regulating gene expression. These mechanisms include the assembly of higher order nucleoprotein complexes and other protein-protein interactions that enhance the functional specificity of transcriptional regulators in lymphocytes.

Animals↗

PubMed1993

Telomeres and telomerases.

The ends of eukaryotic chromosomes are defined by specialized nucleoprotein complexes called telomeres. Telomeres impart stability to the genome and are of general interest due to their unique structure and unconventional mode of synthesis. Recent work has identified new components of the telomere complex and expanded our understanding of the role of terminal structures in maintaining cell viability.

Animals↗

PubMed2000

Modeling DNA deformations.

Recent developments have been made in modeling double-helical DNA at four levels of three-dimensional structure: the all-atom level, whereby an oligonucleotide duplex is surrounded by a shroud of solvent molecules; the base-pair level, with explicit backbone atoms; the mesoscopic level, that is, a few hundred base pairs, with the local duplex conformation described by knowledge-based harmonic energy functions; and the scale of several thousand nucleotides, with the duplex described as an ideal elastic rod. Predictions of the sequence-dependent bending and twisting of the double helix, as well as solvent- and force-induced B-->A and over-stretching conformational transitions, are compared with experimental data. These subtle conformational changes are critical to the functioning of the double helix, including its packaging in the close confines of the cell, the mutual fit of DNA and protein in nucleoprotein complexes, and the effective recognition of base pairs in recombination and transcription.

Animals↗

PubMed2003

The structure of telomeric DNA.

The telomere is a nucleoprotein complex located at the ends of eukaryotic chromosomes. It is essential for maintaining the integrity of the genome. It is not a linear structure and, for much of the cell cycle, telomeric DNA is maintained in a loop structure, which serves to protect the vulnerable ends of chromosomes. Many of the key proteins in the telomere have been identified, although their interplay is still imperfectly understood and structural data are only available on a few. Telomeric DNA itself comprises simple guanine-rich repeats for most of its length, culminating in a short overhang of single-stranded sequence at the extreme 3' ends. This can, at least in vitro, fold into a wide variety of four-stranded quadruplex structures, many of whose arrangements are being revealed by crystallographic and NMR studies.

DNA↗

PubMed2001

Interaction of the virulence protein VirF of Agrobacterium tumefaciens with plant homologs of the yeast Skp1 protein.

The infection of plants by Agrobacterium tumefaciens leads to the formation of crown gall tumors due to the transfer of a nucleoprotein complex into plant cells that is mediated by the virulence (vir) region-encoded transport system (reviewed in [1-5]). In addition, A. tumefaciens secretes the Vir proteins, VirE2 and VirF, directly into plant cells via the same VirB/VirD4 transport system [6], and both assist there in the transformation of normal cells into tumor cells. The function of the 22 kDa VirF protein is not clear. Deletion of the virF gene in A. tumefaciens leads to diminished virulence [7, 8] and can be complemented by the expression of the virF gene in the host plant. This finding indicates that VirF functions within the plant cell [8]. Here, we report that the VirF protein is the first prokaryotic protein with an F box by which it can interact with plant homologs of the yeast Skp1 protein. The presence of the F box turned out to be essential for the biological function of VirF. F box proteins and Skp1p are both subunits of a class of E3 ubiquitin ligases referred to as SCF complexes. Thus, VirF may be involved in the targeted proteolysis of specific host proteins in early stages of the transformation process.

Agrobacterium tumefaciens↗

PubMed1997

Histone acetyltransferases in control.

Several transcriptional regulators have been found to act as enzymes that acetylate histones. The targeted post-translational modification of histones within regulatory nucleoprotein complexes provides an attractive mechanism for controlling transcription within a chromatin environment.

Acetyltransferases↗

PubMed2001

Phosphorylation of viral movement proteins--regulation of cell-to-cell trafficking.

In plants, proteins and nucleoprotein complexes can traffic from cell to cell, via plasmodesmata. Studies based on viral movement proteins (MP) have revealed that such trafficking events are likely to be regulated at the level of protein phosphorylation. Plasmodesmal-associated protein kinases could play a central role in plant defense, in addition to regulating the translatability of endogenous MP-mRNA complexes that function at a supracellular level.

Biological Transport↗

PubMed2001

HMG1 and 2, and related 'architectural' DNA-binding proteins.

The HMG-box proteins, one of the three classes of high mobility group (HMG) chromosomal proteins, bend DNA and bind preferentially to distorted DNA structures. The proteins appear to act primarily as architectural facilitators in the assembly of nucleoprotein complexes; for example, in effecting recombination and in the initiation of transcription. HMG-box proteins might be targeted to particular DNA sites in chromatin by either protein-protein interactions or recognition of specific DNA structures.

Amino Acid Sequence↗

PubMed2001

Computational modeling predicts the structure and dynamics of chromatin fiber.

BACKGROUND: The compact form of the chromatin fiber is a critical regulator of fundamental processes such as transcription and replication. These reactions can occur only when the fiber is unraveled and the DNA strands contained within are exposed to interact with nuclear proteins. While progress on identifying the biochemical mechanisms that control localized folding and hence govern access to genetic information continues, the internal structure of the chromatin fiber, let alone the structural pathways for folding and unfolding, remain unknown. RESULTS: To offer structural insights into how this nucleoprotein complex might be organized, we present a macroscopic computer model describing the mechanics of the chromatin fiber on the polymer level. We treat the core particles as electrostatically charged disks linked via charged elastic DNA segments and surrounded by a microionic hydrodynamic solution. Each nucleosome unit is represented by several hundred charges optimized so that the effective Debye-Hückel electrostatic field matches the field predicted by the nonlinear Poisson-Boltzmann equation. On the basis of Brownian dynamics simulations, we show that oligonucleosomes condense and unfold in a salt-dependent manner analogous to the chromatin fiber. CONCLUSIONS: Our predicted chromatin model shows good agreement with experimental diffusion coefficients and small-angle X-ray scattering data. A fiber of width 30 nm, organized in a compact helical zigzag pattern with about 4 nucleosomes per 10 nm, naturally emerges from a repeating nucleosome folding motif. This fiber has a cross-sectional radius of gyration of R(c) = 8.66 nm, in close agreement with corresponding values for rat thymus and chicken erythrocyte chromatin (8.82 and 8.5 nm, respectively).

Algorithms↗

PubMed1999

Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-beta promoter.

Transcriptional activation of the human interferon-beta (IFN-beta) gene by virus infection requires the assembly of a higher order nucleoprotein complex, the enhanceosome, which consists of the transcriptional activators NF-kappa B (p50/p65), ATF-2/c-jun, IRF-3 and IRF-7, architectural protein HMGI(Y), and the coactivators p300 and CBP. In this report, we show that virus infection of cells results in a dramatic hyperacetylation of histones H3 and H4 that is localized to the IFN-beta promoter. Furthermore, expressing a truncated version of IRF-3, which lacks a p300/CBP interaction domain, suppresses both histone hyperacetylation and activation of the IFN-beta gene. Thus, coactivator-mediated localized hyperacetylation of histones may play a crucial role in inducible gene expression.

Acetylation↗