ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 1
    Publication Date: 2009-09-11
    Description: Phytophthora infestans is the most destructive pathogen of potato and a model organism for the oomycetes, a distinct lineage of fungus-like eukaryotes that are related to organisms such as brown algae and diatoms. As the agent of the Irish potato famine in the mid-nineteenth century, P. infestans has had a tremendous effect on human history, resulting in famine and population displacement. To this day, it affects world agriculture by causing the most destructive disease of potato, the fourth largest food crop and a critical alternative to the major cereal crops for feeding the world's population. Current annual worldwide potato crop losses due to late blight are conservatively estimated at $6.7 billion. Management of this devastating pathogen is challenged by its remarkable speed of adaptation to control strategies such as genetically resistant cultivars. Here we report the sequence of the P. infestans genome, which at approximately 240 megabases (Mb) is by far the largest and most complex genome sequenced so far in the chromalveolates. Its expansion results from a proliferation of repetitive DNA accounting for approximately 74% of the genome. Comparison with two other Phytophthora genomes showed rapid turnover and extensive expansion of specific families of secreted disease effector proteins, including many genes that are induced during infection or are predicted to have activities that alter host physiology. These fast-evolving effector genes are localized to highly dynamic and expanded regions of the P. infestans genome. This probably plays a crucial part in the rapid adaptability of the pathogen to host plants and underpins its evolutionary potential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haas, Brian J -- Kamoun, Sophien -- Zody, Michael C -- Jiang, Rays H Y -- Handsaker, Robert E -- Cano, Liliana M -- Grabherr, Manfred -- Kodira, Chinnappa D -- Raffaele, Sylvain -- Torto-Alalibo, Trudy -- Bozkurt, Tolga O -- Ah-Fong, Audrey M V -- Alvarado, Lucia -- Anderson, Vicky L -- Armstrong, Miles R -- Avrova, Anna -- Baxter, Laura -- Beynon, Jim -- Boevink, Petra C -- Bollmann, Stephanie R -- Bos, Jorunn I B -- Bulone, Vincent -- Cai, Guohong -- Cakir, Cahid -- Carrington, James C -- Chawner, Megan -- Conti, Lucio -- Costanzo, Stefano -- Ewan, Richard -- Fahlgren, Noah -- Fischbach, Michael A -- Fugelstad, Johanna -- Gilroy, Eleanor M -- Gnerre, Sante -- Green, Pamela J -- Grenville-Briggs, Laura J -- Griffith, John -- Grunwald, Niklaus J -- Horn, Karolyn -- Horner, Neil R -- Hu, Chia-Hui -- Huitema, Edgar -- Jeong, Dong-Hoon -- Jones, Alexandra M E -- Jones, Jonathan D G -- Jones, Richard W -- Karlsson, Elinor K -- Kunjeti, Sridhara G -- Lamour, Kurt -- Liu, Zhenyu -- Ma, Lijun -- Maclean, Daniel -- Chibucos, Marcus C -- McDonald, Hayes -- McWalters, Jessica -- Meijer, Harold J G -- Morgan, William -- Morris, Paul F -- Munro, Carol A -- O'Neill, Keith -- Ospina-Giraldo, Manuel -- Pinzon, Andres -- Pritchard, Leighton -- Ramsahoye, Bernard -- Ren, Qinghu -- Restrepo, Silvia -- Roy, Sourav -- Sadanandom, Ari -- Savidor, Alon -- Schornack, Sebastian -- Schwartz, David C -- Schumann, Ulrike D -- Schwessinger, Ben -- Seyer, Lauren -- Sharpe, Ted -- Silvar, Cristina -- Song, Jing -- Studholme, David J -- Sykes, Sean -- Thines, Marco -- van de Vondervoort, Peter J I -- Phuntumart, Vipaporn -- Wawra, Stephan -- Weide, Rob -- Win, Joe -- Young, Carolyn -- Zhou, Shiguo -- Fry, William -- Meyers, Blake C -- van West, Pieter -- Ristaino, Jean -- Govers, Francine -- Birch, Paul R J -- Whisson, Stephen C -- Judelson, Howard S -- Nusbaum, Chad -- BB/E007120/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/G015244/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0400284/Medical Research Council/United Kingdom -- England -- Nature. 2009 Sep 17;461(7262):393-8. doi: 10.1038/nature08358. Epub 2009 Sep 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02141, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19741609" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/genetics ; DNA Transposable Elements/genetics ; DNA, Intergenic/genetics ; Evolution, Molecular ; Genome/*genetics ; Host-Pathogen Interactions/genetics ; Humans ; Ireland ; Molecular Sequence Data ; Necrosis ; Phenotype ; Phytophthora infestans/*genetics/pathogenicity ; Plant Diseases/immunology/*microbiology ; Solanum tuberosum/immunology/*microbiology ; Starvation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2012-11-10
    Description: Phosphine is a small redox-active gas that is used to protect global grain reserves, which are threatened by the emergence of phosphine resistance in pest insects. We find that polymorphisms responsible for genetic resistance cluster around the redox-active catalytic disulfide or the dimerization interface of dihydrolipoamide dehydrogenase (DLD) in insects (Rhyzopertha dominica and Tribolium castaneum) and nematodes (Caenorhabditis elegans). DLD is a core metabolic enzyme representing a new class of resistance factor for a redox-active metabolic toxin. It participates in four key steps of core metabolism, and metabolite profiles indicate that phosphine exposure in mutant and wild-type animals affects these steps differently. Mutation of DLD in C. elegans increases arsenite sensitivity. This specific vulnerability may be exploited to control phosphine-resistant insects and safeguard food security.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlipalius, David I -- Valmas, Nicholas -- Tuck, Andrew G -- Jagadeesan, Rajeswaran -- Ma, Li -- Kaur, Ramandeep -- Goldinger, Anita -- Anderson, Cameron -- Kuang, Jujiao -- Zuryn, Steven -- Mau, Yosep S -- Cheng, Qiang -- Collins, Patrick J -- Nayak, Manoj K -- Schirra, Horst Joachim -- Hilliard, Massimo A -- Ebert, Paul R -- R01NS060129/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 9;338(6108):807-10. doi: 10.1126/science.1224951.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Agri-Science Queensland, Department of Agriculture, Fisheries and Forestry, Ecosciences Precinct, Brisbane, QLD 4001, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23139334" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arsenicals/pharmacology ; Arsenites/pharmacology ; Beetles/drug effects/*enzymology/genetics/metabolism ; Caenorhabditis elegans/drug effects/*enzymology/genetics/metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/metabolism ; Catalytic Domain ; Dihydrolipoamide Dehydrogenase/chemistry/*genetics/metabolism ; Insect Proteins/chemistry/genetics/metabolism ; Insecticide Resistance/*genetics ; *Insecticides/pharmacology ; Metabolic Networks and Pathways ; Molecular Sequence Data ; Mutation ; Oxidation-Reduction ; Pesticides ; *Phosphines/pharmacology ; Polymorphism, Genetic ; Protein Multimerization ; Tribolium/drug effects/*enzymology/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 2010-05-22
    Description: We report the design, synthesis, and assembly of the 1.08-mega-base pair Mycoplasma mycoides JCVI-syn1.0 genome starting from digitized genome sequence information and its transplantation into a M. capricolum recipient cell to create new M. mycoides cells that are controlled only by the synthetic chromosome. The only DNA in the cells is the designed synthetic DNA sequence, including "watermark" sequences and other designed gene deletions and polymorphisms, and mutations acquired during the building process. The new cells have expected phenotypic properties and are capable of continuous self-replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, Daniel G -- Glass, John I -- Lartigue, Carole -- Noskov, Vladimir N -- Chuang, Ray-Yuan -- Algire, Mikkel A -- Benders, Gwynedd A -- Montague, Michael G -- Ma, Li -- Moodie, Monzia M -- Merryman, Chuck -- Vashee, Sanjay -- Krishnakumar, Radha -- Assad-Garcia, Nacyra -- Andrews-Pfannkoch, Cynthia -- Denisova, Evgeniya A -- Young, Lei -- Qi, Zhi-Qing -- Segall-Shapiro, Thomas H -- Calvey, Christopher H -- Parmar, Prashanth P -- Hutchison, Clyde A 3rd -- Smith, Hamilton O -- Venter, J Craig -- New York, N.Y. -- Science. 2010 Jul 2;329(5987):52-6. doi: 10.1126/science.1190719. Epub 2010 May 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The J. Craig Venter Institute, 9704 Medical Center Drive, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20488990" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/analysis ; Base Sequence ; *Bioengineering ; Cloning, Molecular ; DNA, Bacterial/chemical synthesis/genetics ; Escherichia coli/genetics ; Gene Deletion ; Genes, Bacterial ; *Genetic Engineering ; *Genome, Bacterial ; Molecular Sequence Data ; Mycoplasma capricolum/*genetics ; Mycoplasma mycoides/*genetics/growth & development/physiology/ultrastructure ; Phenotype ; Plasmids ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Saccharomyces cerevisiae/genetics ; Transformation, Bacterial
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2015-06-27
    Description: Bacterial adaptive immunity uses CRISPR (clustered regularly interspaced short palindromic repeats)-associated (Cas) proteins together with CRISPR transcripts for foreign DNA degradation. In type II CRISPR-Cas systems, activation of Cas9 endonuclease for DNA recognition upon guide RNA binding occurs by an unknown mechanism. Crystal structures of Cas9 bound to single-guide RNA reveal a conformation distinct from both the apo and DNA-bound states, in which the 10-nucleotide RNA "seed" sequence required for initial DNA interrogation is preordered in an A-form conformation. This segment of the guide RNA is essential for Cas9 to form a DNA recognition-competent structure that is poised to engage double-stranded DNA target sequences. We construe this as convergent evolution of a "seed" mechanism reminiscent of that used by Argonaute proteins during RNA interference in eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jiang, Fuguo -- Zhou, Kaihong -- Ma, Linlin -- Gressel, Saskia -- Doudna, Jennifer A -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2015 Jun 26;348(6242):1477-81. doi: 10.1126/science.aab1452.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. ; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA. ; Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany. ; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA. California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA. Department of Chemistry, University of California, Berkeley, CA 94720, USA. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Innovative Genomics Initiative, University of California, Berkeley, CA 94720, USA. doudna@berkeley.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26113724" target="_blank"〉PubMed〈/a〉
    Keywords: Argonaute Proteins/*chemistry ; Base Sequence ; *CRISPR-Cas Systems ; Caspase 9/*chemistry/genetics ; *Clustered Regularly Interspaced Short Palindromic Repeats ; Crystallography, X-Ray ; DNA/chemistry ; *DNA Cleavage ; Enzyme Activation ; Evolution, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Structure, Tertiary ; RNA Interference ; RNA, Guide/*chemistry ; Streptococcus pyogenes/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...