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  • American Chemical Society  (7)
  • Nature Publishing Group (NPG)  (4)
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  • 1
    Publication Date: 2008-10-17
    Description: Over 30% of proteins are secreted across or integrated into membranes. Their newly synthesized forms contain either cleavable signal sequences or non-cleavable membrane anchor sequences, which direct them to the evolutionarily conserved Sec translocon (SecYEG in prokaryotes and Sec61, comprising alpha-, gamma- and beta-subunits, in eukaryotes). The translocon then functions as a protein-conducting channel. These processes of protein localization occur either at or after translation. In bacteria, the SecA ATPase drives post-translational translocation. The only high-resolution structure of a translocon available so far is that for SecYEbeta from the archaeon Methanococcus jannaschii, which lacks SecA. Here we present the 3.2-A-resolution crystal structure of the SecYE translocon from a SecA-containing organism, Thermus thermophilus. The structure, solved as a complex with an anti-SecY Fab fragment, revealed a 'pre-open' state of SecYE, in which several transmembrane helices are shifted, as compared to the previous SecYEbeta structure, to create a hydrophobic crack open to the cytoplasm. Fab and SecA bind to a common site at the tip of the cytoplasmic domain of SecY. Molecular dynamics and disulphide mapping analyses suggest that the pre-open state might represent a SecYE conformational transition that is inducible by SecA binding. Moreover, we identified a SecA-SecYE interface that comprises SecA residues originally buried inside the protein, indicating that both the channel and the motor components of the Sec machinery undergo cooperative conformational changes on formation of the functional complex.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2590585/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2590585/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsukazaki, Tomoya -- Mori, Hiroyuki -- Fukai, Shuya -- Ishitani, Ryuichiro -- Mori, Takaharu -- Dohmae, Naoshi -- Perederina, Anna -- Sugita, Yuji -- Vassylyev, Dmitry G -- Ito, Koreaki -- Nureki, Osamu -- R01 GM074252/GM/NIGMS NIH HHS/ -- R01 GM074252-04/GM/NIGMS NIH HHS/ -- R01 GM074840/GM/NIGMS NIH HHS/ -- R01 GM074840-04/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 Oct 16;455(7215):988-91. doi: 10.1038/nature07421.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18923527" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/genetics/immunology/*metabolism ; Binding Sites ; Crystallography, X-Ray ; Disulfides/chemistry/metabolism ; Hydrophobic and Hydrophilic Interactions ; Immunoglobulin Fab Fragments/chemistry/immunology ; Methanococcus/chemistry/enzymology ; Models, Biological ; Models, Molecular ; Protein Binding ; Protein Structure, Tertiary ; Thermus thermophilus/*chemistry/*enzymology/genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2008-03-21
    Description: Equal amounts of matter and antimatter are predicted to have been produced in the Big Bang, but our observable Universe is clearly matter-dominated. One of the prerequisites for understanding this elimination of antimatter is the nonconservation of charge-parity (CP) symmetry. So far, two types of CP violation have been observed in the neutral K meson (K(0)) and B meson (B(0)) systems: CP violation involving the mixing between K(0) and its antiparticle (and likewise for B(0) and ), and direct CP violation in the decay of each meson. The observed effects for both types of CP violation are substantially larger for the B(0) meson system. However, they are still consistent with the standard model of particle physics, which has a unique source of CP violation that is known to be too small to account for the matter-dominated Universe. Here we report that the direct CP violation in charged B(+/-)--〉K(+/-)pi(0) decay is different from that in the neutral B(0) counterpart. The direct CP-violating decay rate asymmetry, (that is, the difference between the number of observed B(-)--〉K(-)pi(0) event versus B(+)--〉K(+) pi(0) events, normalized to the sum of these events) is measured to be about +7%, with an uncertainty that is reduced by a factor of 1.7 from a previous measurement. However, the asymmetry for versus B(0)--〉K(+)pi(-) is at the -10% level. Although it is susceptible to strong interaction effects that need further clarification, this large deviation in direct CP violation between charged and neutral B meson decays could be an indication of new sources of CP violation-which would help to explain the dominance of matter in the Universe.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belle Collaboration -- Lin, S-W -- Unno, Y -- Hou, W-S -- Chang, P -- Adachi, I -- Aihara, H -- Akai, K -- Arinstein, K -- Aulchenko, V -- Aushev, T -- Aziz, T -- Bakich, A M -- Balagura, V -- Barberio, E -- Bay, A -- Bedny, I -- Bitenc, U -- Bondar, A -- Bozek, A -- Bracko, M -- Browder, T E -- Chang, M-C -- Chao, Y -- Chen, A -- Chen, K-F -- Chen, W T -- Cheon, B G -- Chiang, C-C -- Chistov, R -- Cho, I-S -- Choi, S-K -- Choi, Y -- Choi, Y K -- Cole, S -- Dalseno, J -- Danilov, M -- Dash, M -- Drutskoy, A -- Eidelman, S -- Epifanov, D -- Fratina, S -- Fujikawa, M -- Furukawa, K -- Gabyshev, N -- Goldenzweig, P -- Golob, B -- Ha, H -- Haba, J -- Hara, T -- Hayasaka, K -- Hayashii, H -- Hazumi, M -- Heffernan, D -- Hokuue, T -- Hoshi, Y -- Hsiung, Y B -- Hyun, H J -- Iijima, T -- Ikado, K -- Inami, K -- Ishikawa, A -- Ishino, H -- Itoh, R -- Iwabuchi, M -- Iwasaki, M -- Iwasaki, Y -- Kah, D H -- Kaji, H -- Kataoka, S U -- Kawai, H -- Kawasaki, T -- Kibayashi, A -- Kichimi, H -- Kikutani, E -- Kim, H J -- Kim, S K -- Kim, Y J -- Kinoshita, K -- Korpar, S -- Kozakai, Y -- Krizan, P -- Krokovny, P -- Kumar, R -- Kuo, C C -- Kuzmin, A -- Kwon, Y-J -- Lee, M J -- Lee, S E -- Lesiak, T -- Li, J -- Liu, Y -- Liventsev, D -- Mandl, F -- Marlow, D -- McOnie, S -- Medvedeva, T -- Mimashi, T -- Mitaroff, W -- Miyabayashi, K -- Miyake, H -- Miyazaki, Y -- Mizuk, R -- Mori, T -- Nakamura, T T -- Nakano, E -- Nakao, M -- Nakazawa, H -- Nishida, S -- Nitoh, O -- Noguchi, S -- Nozaki, T -- Ogawa, S -- Ogawa, Y -- Ohshima, T -- Okuno, S -- Olsen, S L -- Ozaki, H -- Pakhlova, G -- Park, C W -- Park, H -- Peak, L S -- Pestotnik, R -- Peters, M -- Piilonen, L E -- Poluektov, A -- Sahoo, H -- Sakai, Y -- Schneider, O -- Schumann, J -- Schwartz, A J -- Seidl, R -- Senyo, K -- Sevior, M E -- Shapkin, M -- Shen, C P -- Shibuya, H -- Shidara, T -- Shinomiya, S -- Shiu, J-G -- Shwartz, B -- Singh, J B -- Sokolov, A -- Somov, A -- Stanic, S -- Staric, M -- Sumisawa, K -- Sumiyoshi, T -- Suzuki, S -- Tajima, O -- Takasaki, F -- Tamura, N -- Tanaka, M -- Tawada, M -- Taylor, G N -- Teramoto, Y -- Tikhomirov, I -- Trabelsi, K -- Uehara, S -- Ueno, K -- Uglov, T -- Uno, S -- Urquijo, P -- Ushiroda, Y -- Usov, Y -- Varner, G -- Varvell, K E -- Vervink, K -- Villa, S -- Wang, C C -- Wang, C H -- Wang, M-Z -- Watanabe, Y -- Wedd, R -- Wicht, J -- Won, E -- Yabsley, B D -- Yamaguchi, A -- Yamashita, Y -- Yamauchi, M -- Yoshida, M -- Yuan, C Z -- Yusa, Y -- Zhang, C C -- Zhang, Z P -- Zhilich, V -- Zhulanov, V -- Zupanc, A -- England -- Nature. 2008 Mar 20;452(7185):332-5. doi: 10.1038/nature06827.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, National Taiwan University, Taipei, 106, Taiwan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18354478" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2014-04-18
    Description: Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates into the membrane, thereby facilitating membrane protein assembly in bacteria; the homologous proteins Oxa1 and Alb3 have the same function in mitochondria and chloroplasts, respectively. In the bacterial cytoplasmic membrane, YidC functions as an independent insertase and a membrane chaperone in cooperation with the translocon SecYEG. Here we present the crystal structure of YidC from Bacillus halodurans, at 2.4 A resolution. The structure reveals a novel fold, in which five conserved transmembrane helices form a positively charged hydrophilic groove that is open towards both the lipid bilayer and the cytoplasm but closed on the extracellular side. Structure-based in vivo analyses reveal that a conserved arginine residue in the groove is important for the insertion of membrane proteins by YidC. We propose an insertion mechanism for single-spanning membrane proteins, in which the hydrophilic environment generated by the groove recruits the extracellular regions of substrates into the low-dielectric environment of the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumazaki, Kaoru -- Chiba, Shinobu -- Takemoto, Mizuki -- Furukawa, Arata -- Nishiyama, Ken-ichi -- Sugano, Yasunori -- Mori, Takaharu -- Dohmae, Naoshi -- Hirata, Kunio -- Nakada-Nakura, Yoshiko -- Maturana, Andres D -- Tanaka, Yoshiki -- Mori, Hiroyuki -- Sugita, Yuji -- Arisaka, Fumio -- Ito, Koreaki -- Ishitani, Ryuichiro -- Tsukazaki, Tomoya -- Nureki, Osamu -- England -- Nature. 2014 May 22;509(7501):516-20. doi: 10.1038/nature13167. Epub 2014 Apr 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan [2] Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan [3]. ; 1] Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-ku, Kyoto 603-8555, Japan [2]. ; 1] Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan [2] Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. ; Department of Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, Nara 630-0192, Japan. ; Cryobiofrontier Research Center, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka, Iwate 020-8550, Japan. ; Theoretical Molecular Science Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. ; Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. ; SR Life Science Instrumentation Unit, RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan. ; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan. ; Department of Bioengineering Sciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. ; Institute for Virus Research, Kyoto University, Shogoin Kawara-cho, Sakyo-ku, Kyoto 606-8507, Japan. ; Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa 226-8503, Japan. ; Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-ku, Kyoto 603-8555, Japan. ; 1] Department of Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, Nara 630-0192, Japan [2] JST, PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24739968" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/metabolism ; Bacillus/*chemistry ; Bacterial Proteins/*chemistry/*metabolism ; Cell Membrane/chemistry/*metabolism ; Conserved Sequence ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Membrane Transport Proteins/*chemistry/*metabolism ; Molecular Chaperones/chemistry/metabolism ; Protein Folding ; Static Electricity ; Structure-Activity Relationship
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    Electronic ISSN: 1476-4687
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  • 4
    Publication Date: 2014-01-31
    Description: Cultivated bacteria such as actinomycetes are a highly useful source of biomedically important natural products. However, such 'talented' producers represent only a minute fraction of the entire, mostly uncultivated, prokaryotic diversity. The uncultured majority is generally perceived as a large, untapped resource of new drug candidates, but so far it is unknown whether taxa containing talented bacteria indeed exist. Here we report the single-cell- and metagenomics-based discovery of such producers. Two phylotypes of the candidate genus 'Entotheonella' with genomes of greater than 9 megabases and multiple, distinct biosynthetic gene clusters co-inhabit the chemically and microbially rich marine sponge Theonella swinhoei. Almost all bioactive polyketides and peptides known from this animal were attributed to a single phylotype. 'Entotheonella' spp. are widely distributed in sponges and belong to an environmental taxon proposed here as candidate phylum 'Tectomicrobia'. The pronounced bioactivities and chemical uniqueness of 'Entotheonella' compounds provide significant opportunities for ecological studies and drug discovery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, Micheal C -- Mori, Tetsushi -- Ruckert, Christian -- Uria, Agustinus R -- Helf, Maximilian J -- Takada, Kentaro -- Gernert, Christine -- Steffens, Ursula A E -- Heycke, Nina -- Schmitt, Susanne -- Rinke, Christian -- Helfrich, Eric J N -- Brachmann, Alexander O -- Gurgui, Cristian -- Wakimoto, Toshiyuki -- Kracht, Matthias -- Crusemann, Max -- Hentschel, Ute -- Abe, Ikuro -- Matsunaga, Shigeki -- Kalinowski, Jorn -- Takeyama, Haruko -- Piel, Jorn -- England -- Nature. 2014 Feb 6;506(7486):58-62. doi: 10.1038/nature12959. Epub 2014 Jan 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Institute of Microbiology, Eidgenossische Technische Hochschule Zurich, Vladimir-Prelog-Weg 4, 8093 Zurich, Switzerland [2] Kekule Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany [3]. ; 1] Faculty of Science and Engineering, Waseda University Center for Advanced Biomedical Sciences, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan [2]. ; Institute for Genome Research and Systems Biology, Center for Biotechnology, Universitat Bielefeld, Universitatstrasse 25, 33594 Bielefeld, Germany. ; 1] Institute of Microbiology, Eidgenossische Technische Hochschule Zurich, Vladimir-Prelog-Weg 4, 8093 Zurich, Switzerland [2] Kekule Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany. ; Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. ; Department of Botany II, Julius-von-Sachs Institute for Biological Sciences, University of Wurzburg, Julius-von-Sachs-Platz 3, 97082 Wurzburg, Germany. ; Kekule Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany. ; Department of Earth and Environmental Sciences, Palaeontology and Geobiology, Ludwig Maximilians University Munich, Richard-Wagner-Strasse 10, 80333 Munich, Germany. ; Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, California 94598, USA. ; Institute of Microbiology, Eidgenossische Technische Hochschule Zurich, Vladimir-Prelog-Weg 4, 8093 Zurich, Switzerland. ; Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. ; Faculty of Science and Engineering, Waseda University Center for Advanced Biomedical Sciences, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24476823" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biosynthetic Pathways/genetics ; Deltaproteobacteria/*classification/genetics/*metabolism/physiology ; *Drug Discovery ; Environmental Microbiology ; Genes, Bacterial/genetics ; Genome, Bacterial/genetics ; Metagenomics ; Molecular Sequence Data ; Multigene Family/genetics ; Peptides/metabolism ; Polyketides/metabolism ; Porifera/metabolism/microbiology ; Single-Cell Analysis ; Symbiosis
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    Electronic ISSN: 1476-4687
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  • 5
    Publication Date: 2008-09-09
    Print ISSN: 0897-4756
    Electronic ISSN: 1520-5002
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
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  • 6
    Publication Date: 2001-12-01
    Print ISSN: 0021-8561
    Electronic ISSN: 1520-5118
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
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  • 7
    Publication Date: 1999-09-01
    Print ISSN: 0020-1669
    Electronic ISSN: 1520-510X
    Topics: Chemistry and Pharmacology
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  • 8
  • 9
  • 10
    Publication Date: 1999-06-25
    Print ISSN: 0024-9297
    Electronic ISSN: 1520-5835
    Topics: Chemistry and Pharmacology , Physics
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