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  • 1
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    MglA regulates polarity of gliding in M. xanthus [Microbiology] (2015)
    National Academy of Sciences
    Details
    Publication Date: 2015-01-15
    Description: Gliding motility in Myxococcus xanthus is powered by flagella stator homologs that move in helical trajectories using proton motive force. The Frz chemosensory pathway regulates the cell polarity axis through MglA, a Ras family GTPase; however, little is known about how MglA establishes the polarity of gliding, because the gliding...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    A conformational checkpoint between DNA binding and cleavage by CRISPR-Cas9 (2017)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2017-08-05
    Description: The Cas9 endonuclease is widely used for genome engineering applications by programming its single-guide RNA, and ongoing work is aimed at improving the accuracy and efficiency of DNA targeting. DNA cleavage of Cas9 is controlled by the conformational state of the HNH nuclease domain, but the mechanism that governs HNH activation at on-target DNA while reducing cleavage activity at off-target sites remains poorly understood. Using single-molecule Förster resonance energy transfer, we identified an intermediate state of Streptococcus pyogenes Cas9, representing a conformational checkpoint between DNA binding and cleavage. Upon DNA binding, the HNH domain transitions between multiple conformations before docking into its active state. HNH docking requires divalent cations, but not strand scission, and this docked conformation persists following DNA cleavage. Sequence mismatches between the DNA target and guide RNA prevent transitions from the checkpoint intermediate to the active conformation, providing selective avoidance of DNA cleavage at stably bound off-target sites.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Strength of Selection Pressure Is an Important Parameter Contributing to the Complexity of Antibiotic Resistance Evolution (2014)
    Oxford University Press
    Details
    Publication Date: 2014-08-20
    Description: Revealing the genetic changes responsible for antibiotic resistance can be critical for developing novel antibiotic therapies. However, systematic studies correlating genotype to phenotype in the context of antibiotic resistance have been missing. In order to fill in this gap, we evolved 88 isogenic Escherichia coli populations against 22 antibiotics for 3 weeks. For every drug, two populations were evolved under strong selection and two populations were evolved under mild selection. By quantifying evolved populations’ resistances against all 22 drugs, we constructed two separate cross-resistance networks for strongly and mildly selected populations. Subsequently, we sequenced representative colonies isolated from evolved populations for revealing the genetic basis for novel phenotypes. Bacterial populations that evolved resistance against antibiotics under strong selection acquired high levels of cross-resistance against several antibiotics, whereas other bacterial populations evolved under milder selection acquired relatively weaker cross-resistance. In addition, we found that strongly selected strains against aminoglycosides became more susceptible to five other drug classes compared with their wild-type ancestor as a result of a point mutation on TrkH, an ion transporter protein. Our findings suggest that selection strength is an important parameter contributing to the complexity of antibiotic resistance problem and use of high doses of antibiotics to clear infections has the potential to promote increase of cross-resistance in clinics.
    Print ISSN: 0737-4038
    Electronic ISSN: 1537-1719
    Topics: Biology
    Published by Oxford University Press
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  • 4
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    Detection of the water reservoir in a forming planetary system (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-10-25
    Description: Icy bodies may have delivered the oceans to the early Earth, yet little is known about water in the ice-dominated regions of extrasolar planet-forming disks. The Heterodyne Instrument for the Far-Infrared on board the Herschel Space Observatory has detected emission lines from both spin isomers of cold water vapor from the disk around the young star TW Hydrae. This water vapor likely originates from ice-coated solids near the disk surface, hinting at a water ice reservoir equivalent to several thousand Earth oceans in mass. The water's ortho-to-para ratio falls well below that of solar system comets, suggesting that comets contain heterogeneous ice mixtures collected across the entire solar nebula during the early stages of planetary birth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogerheijde, Michiel R -- Bergin, Edwin A -- Brinch, Christian -- Cleeves, L Ilsedore -- Fogel, Jeffrey K J -- Blake, Geoffrey A -- Dominik, Carsten -- Lis, Dariusz C -- Melnick, Gary -- Neufeld, David -- Panic, Olja -- Pearson, John C -- Kristensen, Lars -- Yildiz, Umut A -- van Dishoeck, Ewine F -- New York, N.Y. -- Science. 2011 Oct 21;334(6054):338-40. doi: 10.1126/science.1208931.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Leiden Observatory, Leiden University, Post Office Box 9513, 2300 RA Leiden, Netherlands. michiel@strw.leidenuniv.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22021851" target="_blank"〉PubMed〈/a〉
    Keywords: Evolution, Planetary ; Extraterrestrial Environment ; *Ice ; *Planets ; *Stars, Celestial ; *Steam
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving approximately 37 nanometers for each adenosine triphosphate hydrolyzed. We have labeled myosin V with a single fluorophore at different positions in the light-chain domain and measured the step size with a standard deviation of 〈1.5 nanometers, with 0.5-second temporal resolution, and observation times of minutes. The step size alternates between 37 + 2x nm and 37 - 2x, where x is the distance along the direction of motion between the dye and the midpoint between the two heads. These results strongly support a hand-over-hand model of motility, not an inchworm model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- Forkey, Joseph N -- McKinney, Sean A -- Ha, Taekjip -- Goldman, Yale E -- Selvin, Paul R -- AR26846/AR/NIAMS NIH HHS/ -- AR44420/AR/NIAMS NIH HHS/ -- GM65367/GM/NIGMS NIH HHS/ -- PHS 5 T32 GM08276/PH/PHPPO CDC HHS/ -- R01 GM065367/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2061-5. Epub 2003 Jun 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791999" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Calmodulin ; Carbocyanines/metabolism ; Catalytic Domain ; Dna ; Fluorescence ; Fluorescent Dyes/metabolism ; Kinetics ; Mathematics ; Microscopy, Fluorescence ; *Models, Biological ; Molecular Motor Proteins/chemistry/*metabolism ; Myosin Light Chains/chemistry/metabolism ; Myosin Type V/chemistry/*metabolism ; Protein Structure, Tertiary ; Rhodamines/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Kinesin walks hand-over-hand (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-20
    Description: Kinesin is a processive motor that takes 8.3-nm center-of-mass steps along microtubules for each adenosine triphosphate hydrolyzed. Whether kinesin moves by a "hand-over-hand" or an "inchworm" model has been controversial. We have labeled a single head of the kinesin dimer with a Cy3 fluorophore and localized the position of the dye to within 2 nm before and after a step. We observed that single kinesin heads take steps of 17.3 +/- 3.3 nm. A kinetic analysis of the dwell times between steps shows that the 17-nm steps alternate with 0-nm steps. These results strongly support a hand-over-hand mechanism, and not an inchworm mechanism. In addition, our results suggest that kinesin is bound by both heads to the microtubule while it waits for adenosine triphosphate in between steps.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- Tomishige, Michio -- Vale, Ronald D -- Selvin, Paul R -- AR42895/AR/NIAMS NIH HHS/ -- AR44420/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):676-8. Epub 2003 Dec 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14684828" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate ; Carbocyanines ; Dimerization ; Fluorescence ; Fluorescent Dyes ; Humans ; Kinesin/chemistry/genetics/*metabolism ; Kinetics ; Microtubules/*metabolism ; *Models, Biological ; Models, Molecular ; Molecular Motor Proteins/chemistry/genetics/*metabolism ; Mutation ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    GE Prize winner. How molecular motors move (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):792-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94107, USA. yildiz@cmp.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469911" target="_blank"〉PubMed〈/a〉
    Keywords: Awards and Prizes ; Binding Sites ; Calmodulin/metabolism ; Carbocyanines ; *Fluorescent Dyes ; Humans ; Kinesin/*physiology ; Models, Biological ; Molecular Motor Proteins/*physiology ; Movement ; Myosin Heavy Chains/*physiology ; Myosin Type V/*physiology ; Nanotechnology ; Rhodamines
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-12-14
    Description: Cytoplasmic dynein is a homodimeric AAA+ motor that transports a multitude of cargos toward the microtubule minus end. How the two catalytic head domains interact and move relative to each other during processive movement is unclear. Here, we tracked the relative positions of both heads with nanometer precision and directly observed the heads moving independently along the microtubule. The heads remained widely separated, and their stepping behavior varied as a function of interhead separation. One active head was sufficient for processive movement, and an active head could drag an inactive partner head forward. Thus, dynein moves processively without interhead coordination, a mechanism fundamentally distinct from the hand-over-hand stepping of kinesin and myosin.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4033606/" 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/PMC4033606/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeWitt, Mark A -- Chang, Amy Y -- Combs, Peter A -- Yildiz, Ahmet -- GM08295/GM/NIGMS NIH HHS/ -- GM094522/GM/NIGMS NIH HHS/ -- R01 GM094522/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jan 13;335(6065):221-5. doi: 10.1126/science.1215804. Epub 2011 Dec 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22157083" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Cytoplasm/*metabolism ; Dyneins/*chemistry/*metabolism ; Microtubules/*metabolism ; Models, Biological ; Models, Molecular ; Protein Multimerization ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
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    Structural, electrical and optical characterization of InGaN layers grown by MOVPE (2009)
    Institute of Physics
    Details
    Publication Date: 2009-09-01
    Print ISSN: 1674-1056
    Electronic ISSN: 2058-3834
    Topics: Physics
    Published by Institute of Physics
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  • 10
    Electronic Resource
    Electronic Resource
    Braid group related algebras, their representations and generalized hydrogenlike spectra (1994)
    College Park, Md. : American Institute of Physics (AIP)
    Journal of Mathematical Physics 35 (1994), S. 3074-3088 
    Details
    ISSN: 1089-7658
    Source: AIP Digital Archive
    Topics: Mathematics , Physics
    Notes: Representations of the n-braid group where generators are given by matrices whose elements belong to a noncommutative algebra are discussed. Representation of this algebra in a Hilbert space generalizes the Burau representation. Two algebras which are closely related and are physically indistinguishable provided that a particular eigenvalue is fine tuned are discussed. It is shown that the generalized oscillator system given by one of the algebras generates a hydrogenlike spectrum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.530506
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    Paper (German National Licenses)
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