placeholder
and
and

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Document type
Language
Year
  • 1
    Language: English
    In: Nucleic acids research, 2020-02-20, Vol.48 (3), p.1271-1284
    Description: Abstract The healing of broken chromosomes by de novo telomere addition, while a normal developmental process in some organisms, has the potential to cause extensive loss of heterozygosity, genetic disease, or cell death. However, it is unclear how de novo telomere addition (dnTA) is regulated at DNA double-strand breaks (DSBs). Here, using a non-essential minichromosome in fission yeast, we identify roles for the HR factors Rqh1 helicase, in concert with Rad55, in suppressing dnTA at or near a DSB. We find the frequency of dnTA in rqh1Δ rad55Δ cells is reduced following loss of Exo1, Swi5 or Rad51. Strikingly, in the absence of the distal homologous chromosome arm dnTA is further increased, with nearly half of the breaks being healed in rqh1Δ rad55Δ or rqh1Δ exo1Δ cells. These findings provide new insights into the genetic context of highly efficient dnTA within HR intermediates, and how such events are normally suppressed to maintain genome stability.
    Subject(s): Chromosomes, Fungal - genetics ; DNA Breaks, Double-Stranded ; DNA Helicases - genetics ; DNA-Binding Proteins - genetics ; Exodeoxyribonucleases - genetics ; Gene Expression Regulation, Fungal - genetics ; Genome Integrity, Repair and ; Genome, Fungal - genetics ; Genomic Instability - genetics ; Loss of Heterozygosity - genetics ; Rad51 Recombinase - genetics ; Recombinational DNA Repair - genetics ; Schizosaccharomyces - genetics ; Schizosaccharomyces pombe Proteins - genetics ; Telomere - genetics
    ISSN: 0305-1048
    E-ISSN: 1362-4962
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Language: English
    In: Nucleic acids research, 2014-05-01, Vol.42 (9), p.5644-5656
    Description: DNA double-strand breaks (DSBs) can cause chromosomal rearrangements and extensive loss of heterozygosity (LOH), hallmarks of cancer cells. Yet, how such events are normally suppressed is unclear. Here we identify roles for the DNA damage checkpoint pathway in facilitating homologous recombination (HR) repair and suppressing extensive LOH and chromosomal rearrangements in response to a DSB. Accordingly, deletion of Rad3ATR, Rad26ATRIP, Crb253BP1 or Cdc25 overexpression leads to reduced HR and increased break-induced chromosome loss and rearrangements. We find the DNA damage checkpoint pathway facilitates HR, in part, by promoting break-induced Cdt2-dependent nucleotide synthesis. We also identify additional roles for Rad17, the 9-1-1 complex and Chk1 activation in facilitating break-induced extensive resection and chromosome loss, thereby suppressing extensive LOH. Loss of Rad17 or the 9-1-1 complex results in a striking increase in break-induced isochromosome formation and very low levels of chromosome loss, suggesting the 9-1-1 complex acts as a nuclease processivity factor to facilitate extensive resection. Further, our data suggest redundant roles for Rad3ATR and Exo1 in facilitating extensive resection. We propose that the DNA damage checkpoint pathway coordinates resection and nucleotide synthesis, thereby promoting efficient HR repair and genome stability.
    Subject(s): Cell Cycle Checkpoints ; Checkpoint Kinase 2 - metabolism ; Chromosomes, Fungal - genetics ; Comparative Genomic Hybridization ; DNA Breaks, Double-Stranded ; DNA Cleavage ; Exodeoxyribonucleases - metabolism ; Genome Integrity, Repair and ; Genome, Fungal ; Genomic Instability ; Loss of Heterozygosity ; Nucleotides - biosynthesis ; Recombinational DNA Repair ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins - metabolism
    ISSN: 0305-1048
    E-ISSN: 1362-4962
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Language: English
    In: Molecular and Cellular Biology, 2007-11-01, Vol.27 (21), p.7745-7757
    Description: Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
    Subject(s): Alleles ; Base Sequence ; Chromosomes, Fungal - metabolism ; Crossing Over, Genetic ; DNA Breaks, Double-Stranded ; DNA Repair ; Genetic Markers ; Loss of Heterozygosity - genetics ; Models, Genetic ; Molecular Sequence Data ; Multiprotein Complexes - metabolism ; Mutation - genetics ; Phylogeny ; Rad51 Recombinase - metabolism ; Recombination, Genetic ; Schizosaccharomyces - cytology ; Schizosaccharomyces - genetics ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins - metabolism ; Telomere - metabolism ; Translocation, Genetic
    ISSN: 0270-7306
    E-ISSN: 1098-5549
    Source: HighWire Press (Free Journals)
    Source: Hellenic Academic Libraries Link
    Source: PubMed Central
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Language: English
    In: Journal of medical microbiology, 2001-07-01, Vol.50 (7), p.613-619
    Description: Program in Infectious Diseases, Department of Microbiology, Faculty of Medicine, National University of Singapore, Singapore Corresponding author: Dr K.P. Song (e-mail: micskp{at}nus.edu.sg ). Received 23 Aug. 2000; revised version accepted 11 Dec. 2000. Abstract Toxigenic strains of Clostridium difficile produce two large bacterial toxins called toxins A (TcdA) and B (TcdB). tcdA and tcdB genes are located on the pathogenicity locus of C. difficile , a unique characteristic of toxigenic strains of this species. Intergenic to the two toxin genes is tcdE , a small 501-bp open reading frame of unknown function. Expression of the tcdE gene in Escherichia coli caused bacterial cell death. Computational analysis of the amino acid sequence of TcdE revealed structural features that are strikingly similar to a class of bacteriophage proteins called holins. Holins are cytolytic proteins that cause lysis of bacterial hosts to effect the release of progeny phages. Further analysis of the recombinant clone expressing TcdE by transmission electron microscopy confirmed that the site of action of TcdE is on the bacterial cell membrane. The results provide evidence that TcdE is structurally and functionally similar to holin proteins. TcdE may function as a lytic protein to facilitate the release of TcdA and TcdB to the extracellular environment, as these toxins lack signal peptide.
    Subject(s): Amino Acid Sequence ; Bacterial Proteins - genetics ; Bacterial Proteins - physiology ; Biological and medical sciences ; Clostridium difficile ; Clostridium difficile - genetics ; Clostridium difficile - pathogenicity ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Microscopy, Electron ; Molecular Sequence Data ; N-Acetylmuramoyl-L-alanine Amidase ; Open Reading Frames ; tcdE gene
    ISSN: 0022-2615
    E-ISSN: 1473-5644
    Source: Alma/SFX Local Collection
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Language: English
    In: Journal of medical virology, 2008-11, Vol.80 (11), p.1972-1983
    Description: The hemagglutinin (HA) of influenza A virus plays an essential role in mediating the entry of the virus into host cells. Here, recombinant full‐length HA5 protein from a H5N1 isolate (A/chicken/hatay/2004(H5N1)) was expressed and purified from the baculovirus‐insect cell system. As expected, full‐length HA5 elicits strong neutralizing antibodies, as evaluated in micro‐neutralization tests using HA5 pseudotyped lentiviral particles. In addition, two fragments of HA5 were expressed in bacteria and the N‐terminal fragment, covering the ectodomain before the HA1/HA2 polybasic cleavage site, was found to elicit neutralizing antibodies. But the C‐terminal fragment, which covers the remaining portion of the ectodomain, did not. Neutralizing titer of the anti‐serum against the N‐terminal fragment is only four times lower than the anti‐serum against the full‐length HA5 protein. Using a novel membrane fusion assay, the abilities of these antibodies to block membrane fusion were found to correlate well with the neutralization activities. J. Med. Virol. 80:1972–1983, 2008. © 2008 Wiley‐Liss, Inc.
    Subject(s): Animals ; Antibodies, Viral - blood ; Bacteria ; Baculoviridae - genetics ; baculovirus ; Biological and medical sciences ; Cell Line ; Fundamental and applied biological sciences. Psychology ; Genetic Vectors ; HA5 pseudotyped lentiviral particles ; Hemagglutinin Glycoproteins, Influenza Virus - genetics ; Hemagglutinin Glycoproteins, Influenza Virus - immunology ; Human viral diseases ; Infectious diseases ; Influenza A virus ; Influenza A Virus, H5N1 Subtype - genetics ; Influenza A Virus, H5N1 Subtype - immunology ; Influenza Vaccines - immunology ; Medical sciences ; membrane fusion ; Microbiology ; Miscellaneous ; Neutralization Tests ; neutralizing antibodies ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Spodoptera ; Viral diseases ; Virology
    ISSN: 0146-6615
    E-ISSN: 1096-9071
    Source: Hellenic Academic Libraries Link
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    Language: English
    In: Journal of medical virology, 2010-03, Vol.82 (3), p.467-475
    Description: The non‐structural protein NS1 of the influenza A virus is a good target for the development of diagnostic assays. In this study, three NS1 monoclonal antibodies (mAbs) were generated by using recombinant NS1 protein of H5N1 virus and found to bind both the native and denatured forms of NS1. Two of the mAbs, 6A4 and 2H6, bind NS1 of three different strains of influenza A virus, namely H1N1, H3N2, and H5N1. Epitope mapping revealed that residues 42–53 of H5N1 NS1 are essential for the interaction with both mAbs. Between the three strains, there is only one amino acid difference in this domain, which is consistent with the observed cross‐reactivities. On the other hand, mAb 1G1 binds to residues 206–215 of H5N1 NS1 and does not bind NS1 of H1N1 or H3N2. Furthermore, all three mAbs detected NS1 proteins expressed in virus infected MDCK cells and indirect immunofluorescence staining with mAbs 6A4 and 2H6 provided an alternative method for viral titer determination. Quantifying the numbers of fluorescent foci units yielded viral titers for three different isolates of H5N1 virus that are highly comparable to that obtained by observing cytopathic effect induced by virus infection. Importantly, this alternative method yields results at 1 day post‐infection while the conventional method using cytopathic effect yields results at 3 days post‐infection. The results showed that this new panel of NS1 antibodies can detect NS1 protein expressed during viral infection and can be used for fast and easy titration of influenza A virus. J. Med. Virol. 82:467–475, 2010. © 2010 Wiley‐Liss, Inc.
    Subject(s): Animals ; Antibodies, Monoclonal ; Antibodies, Viral ; Biological and medical sciences ; Cell Line ; Clinical Laboratory Techniques - methods ; Cytopathogenic Effect, Viral ; diagnostic assay ; Dogs ; Epitope Mapping ; Fundamental and applied biological sciences. Psychology ; H5N1 ; Human viral diseases ; Humans ; Infectious diseases ; Influenza A virus - classification ; Influenza A virus - immunology ; Influenza A virus - isolation & purification ; Influenza A Virus, H1N1 Subtype - immunology ; Influenza A Virus, H5N1 Subtype - immunology ; Influenza, Human - diagnosis ; Medical sciences ; Medicin och hälsovetenskap ; Microbiology ; Miscellaneous ; non-structural protein NS1 ; Time Factors ; Viral diseases ; Viral Nonstructural Proteins - immunology ; viral titration ; Virology ; Virology - methods
    ISSN: 0146-6615
    ISSN: 1096-9071
    E-ISSN: 1096-9071
    Source: Hellenic Academic Libraries Link
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Language: English
    In: The Journal of biological chemistry, 1998-09-11, Vol.273 (37), p.23621-23624
    Description: The interleukin-1β-converting enzyme-like protease precursor, pro-caspase-1, has an N-terminal prodomain that is removed during cleavage activation of the protease. Here we show that tumor necrosis factor treatment of HeLa cells induced apoptosis without detectable proteolytic activation of caspase-1 in the cytosol. Instead, tumor necrosis factor induced the translocation of pro-caspase-1 to the nucleus where it was proteolytically activated, releasing the intact prodomain. We identified a nuclear localization signal in the prodomain, which was required for translocation of both pro-caspase-1 as well as its prodomain to the nucleus. Surprisingly, transfected MCF-7 carcinoma or embryonic kidney 293T cells expressing the prodomain alone underwent apoptosis. These results show that death signal-induced nuclear targeting is a novel activity of a caspase prodomain and indicate that caspase-1 and its prodomain may have hitherto unsuspected nuclear functions in apoptosis.
    Subject(s): Amino Acid Sequence ; Apoptosis ; Breast Neoplasms ; Caspase 1 ; Caspases ; Cell Line ; Cell Nucleus - enzymology ; Cysteine Endopeptidases - metabolism ; Cytosol - enzymology ; Enzyme Activation ; Enzyme Precursors - metabolism ; Epitopes - analysis ; Epitopes - chemistry ; Female ; HeLa Cells ; Humans ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Polymerase Chain Reaction ; Protein Processing, Post-Translational ; Recombinant Proteins - metabolism ; Recombinant Proteins - pharmacology ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha - pharmacology
    ISSN: 0021-9258
    E-ISSN: 1083-351X
    Source: HighWire Press (Free Journals)
    Source: Alma/SFX Local Collection
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    Language: English
    In: Applied and Environmental Microbiology, 1996-06, Vol.62 (6), p.2174-2176
    Description: A new gene encoding a 35.8-kDa mosquitocidal toxin (Mtx3; 326 amino acids) was isolated from Bacillus sphaericus SSII-1 DNA. Mtx3 is a new type of mosquitocidal toxin with homology to the Mtx2 mosquitocidal toxin of B. sphaericus SSII-1, the epsilon-toxin of Clostridium perfringens, and the cytotoxin of Pseudomonas aeruginosa. The mtx3 gene is highly conserved and widely distributed in both high- and low-toxicity mosquito larvicidal strains of B. sphaericus
    Subject(s): AEDES AEGYPTI ; Amino Acid Sequence ; Analysis ; Bacillus (Bacteria) ; Bacillus - genetics ; BACILLUS SPHAERICUS ; Bacteria ; Bacterial toxins ; Bacterial Toxins - chemistry ; Bacterial Toxins - genetics ; Base Sequence ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; CLONACION ; CLONAGE ; Clostridium perfringens ; Clostridium perfringens - genetics ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; Conserved Sequence ; CULEX QUINQUEFASCIATUS ; DNA, Bacterial - genetics ; ESCHERICHIA COLI ; Escherichia coli - genetics ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fundamental and applied biological sciences. Psychology ; GENE ; GENES ; Genes, Bacterial ; Genetic aspects ; Genetics ; Glutathione Transferase - genetics ; INSECTICIDAS ; INSECTICIDE ; LARVAS ; LARVE ; Mission oriented research ; Molecular Sequence Data ; Molecular Weight ; Mosquitoes ; Pseudomonas aeruginosa ; Pseudomonas aeruginosa - genetics ; Recombinant Fusion Proteins - genetics ; RNA, Bacterial - genetics ; RNA, Ribosomal, 16S - genetics ; SECUENCIA NUCLEOTIDICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; TOXINAS ; TOXINE ; TRANSFERENCIA DE GENES ; TRANSFERT DE GENE
    ISSN: 0099-2240
    E-ISSN: 1098-5336
    Source: HighWire Press (Free Journals)
    Source: Hellenic Academic Libraries Link
    Source: PubMed Central
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    Language: English
    In: The Journal of biological chemistry, 1996-06-14, Vol.271 (24), p.14183-14187
    Description: Five different mosquitocidal toxin (mtx2) gene homologs have been cloned from eight Bacillus sphaericus strains. Pairwise comparisons of the predicted amino acid sequences show between four and eight substitutions compared with the prototype Mtx2 from B. sphaericus strain SSII-1. Mtx2 from strain SSII-1 was approximately 7-fold more toxic to Culex mosquito larvae than the Mtx2 homolog from B. sphaericus strain 31-2. Conversely, Mtx2 from strain 31-2 was approximately 100-fold more toxic to Aedes mosquito larvae than Mtx2 from strain SSII-1. Lys224 in Mtx2 was found to be the most important amino acid for toxicity to Culex larvae, and substitution of Lys224 with threonine abolished the toxicity of Mtx2 from strain SSII-1 to these larvae. In complete contrast, Thr224 was found to be crucial for the toxicity of Mtx2 from strain 31-2 to Aedes larvae, and substitution of Thr224 with lysine caused a approximately 100-fold drop in toxicity to these larvae. Thus, amino acid 224 in the Mtx2 family of mosquitocidal toxins is an unusual and important determinant of mosquito larvicidal activity and host range
    Subject(s): Aedes ; Amino Acid Sequence ; Animals ; Bacillus - genetics ; Bacillus - metabolism ; BACILLUS SPHAERICUS ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - toxicity ; Bacterial Toxins ; Base Sequence ; CLONACION ; CLONAGE ; Cloning, Molecular ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; Culex ; CULEX QUINQUEFASCIATUS ; Culicidae ; Diptera ; DNA Primers ; GENE ; GENES ; Genes, Bacterial ; HOTE ; HUESPEDES ; INSECTICIDAS ; INSECTICIDE ; Insecticides ; Larva ; LARVAS ; LARVE ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; PESTICIDE BACTERIEN ; PLAGUICIDAS BACTERIANOS ; Polymerase Chain Reaction ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - toxicity ; SECUENCIA NUCLEOTIDICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; Species Specificity ; TOXICIDAD ; TOXICITE ; TOXINAS BACTERIANAS ; TOXINE BACTERIENNE
    ISSN: 0021-9258
    E-ISSN: 1083-351X
    Source: HighWire Press (Free Journals)
    Source: Alma/SFX Local Collection
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...