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  1. Article ; Online: Correction: The structure of the Ctf19c/CCAN from budding yeast.

    Hinshaw, Stephen M / Harrison, Stephen C

    eLife

    2020  Volume 9

    Language English
    Publishing date 2020-03-05
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.56553
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  2. Article ; Online: Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface.

    Zahm, Jacob A / Jenni, Simon / Harrison, Stephen C

    Open biology

    2023  Volume 13, Issue 3, Page(s) 220378

    Abstract: ... occurs instead at a hinge closer to the globular head. Conserved stretches of the Dam1 C terminus bind ...

    Abstract The conserved Ndc80 kinetochore complex, Ndc80c, is the principal link between mitotic spindle microtubules and centromere-associated proteins. We used AlphaFold 2 (AF2) to obtain predictions of the Ndc80 'loop' structure and of the Ndc80 : Nuf2 globular head domains that interact with the Dam1 subunit of the heterodecameric DASH/Dam1 complex (Dam1c). The predictions guided design of crystallizable constructs, with structures close to the predicted ones. The Ndc80 'loop' is a stiff, α-helical 'switchback' structure; AF2 predictions and positions of preferential cleavage sites indicate that flexibility within the long Ndc80c rod occurs instead at a hinge closer to the globular head. Conserved stretches of the Dam1 C terminus bind Ndc80c such that phosphorylation of Dam1 serine residues 257, 265 and 292 by the mitotic kinase Ipl1/Aurora B can release this contact during error correction of mis-attached kinetochores. We integrate the structural results presented here into our current molecular model of the kinetochore-microtubule interface. The model illustrates how multiple interactions between Ndc80c, DASH/Dam1c and the microtubule lattice stabilize kinetochore attachments.
    MeSH term(s) Aurora Kinase B/metabolism ; Cell Cycle Proteins ; Centromere/genetics ; Centromere/metabolism ; Furylfuramide ; Kinetochores/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Aurora Kinase B (EC 2.7.11.1) ; Cell Cycle Proteins ; DAM1 protein, S cerevisiae ; Furylfuramide (054NR2135Y) ; IPL1 protein, S cerevisiae (EC 2.7.11.1) ; Microtubule-Associated Proteins ; NDC80 protein, S cerevisiae ; Nuclear Proteins ; NUF2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2023-03-08
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2630944-0
    ISSN 2046-2441 ; 2046-2441
    ISSN (online) 2046-2441
    ISSN 2046-2441
    DOI 10.1098/rsob.220378
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  3. Article ; Online: Pictures of the prologue to neurotransmitter release.

    Harrison, Stephen C

    Proceedings of the National Academy of Sciences of the United States of America

    2017  Volume 114, Issue 34, Page(s) 8920–8922

    Language English
    Publishing date 2017-08-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1712038114
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  4. Article ; Online: Structure of the Ndc80 complex and its interactions at the yeast kinetochore–microtubule interface

    Jacob A. Zahm / Simon Jenni / Stephen C. Harrison

    Open Biology, Vol 13, Iss

    2023  Volume 3

    Abstract: ... occurs instead at a hinge closer to the globular head. Conserved stretches of the Dam1 C terminus bind ...

    Abstract The conserved Ndc80 kinetochore complex, Ndc80c, is the principal link between mitotic spindle microtubules and centromere-associated proteins. We used AlphaFold 2 (AF2) to obtain predictions of the Ndc80 ‘loop’ structure and of the Ndc80 : Nuf2 globular head domains that interact with the Dam1 subunit of the heterodecameric DASH/Dam1 complex (Dam1c). The predictions guided design of crystallizable constructs, with structures close to the predicted ones. The Ndc80 ‘loop’ is a stiff, α-helical ‘switchback’ structure; AF2 predictions and positions of preferential cleavage sites indicate that flexibility within the long Ndc80c rod occurs instead at a hinge closer to the globular head. Conserved stretches of the Dam1 C terminus bind Ndc80c such that phosphorylation of Dam1 serine residues 257, 265 and 292 by the mitotic kinase Ipl1/Aurora B can release this contact during error correction of mis-attached kinetochores. We integrate the structural results presented here into our current molecular model of the kinetochore–microtubule interface. The model illustrates how multiple interactions between Ndc80c, DASH/Dam1c and the microtubule lattice stabilize kinetochore attachments.
    Keywords cell division ; chromosome segregation ; kinetochore ; Ndc80 complex ; Dam1 complex ; structure prediction ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2023-03-01T00:00:00Z
    Publisher The Royal Society
    Document type Article ; Online
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  5. Article ; Online: The Structural Basis for Kinetochore Stabilization by Cnn1/CENP-T.

    Hinshaw, Stephen M / Harrison, Stephen C

    Current biology : CB

    2020  Volume 30, Issue 17, Page(s) 3425–3431.e3

    Abstract: Chromosome segregation depends on a regulated connection between spindle microtubules and centromeric DNA. The kinetochore mediates this connection and ensures it persists during anaphase, when sister chromatids must transit into daughter cells ... ...

    Abstract Chromosome segregation depends on a regulated connection between spindle microtubules and centromeric DNA. The kinetochore mediates this connection and ensures it persists during anaphase, when sister chromatids must transit into daughter cells uninterrupted. The Ctf19 complex (Ctf19c) forms the centromeric base of the kinetochore in budding yeast. Biochemical experiments show that Ctf19c members associate hierarchically when purified from cell extract [1], an observation that is mostly explained by the structure of the complex [2]. The Ctf3 complex (Ctf3c), which is not required for the assembly of most other Ctf19c factors, disobeys the biochemical assembly hierarchy when observed in dividing cells that lack more basal components [3]. Thus, the biochemical experiments do not completely recapitulate the logic of centromeric Ctf19c assembly. We now present a high-resolution structure of the Ctf3c bound to the Cnn1-Wip1 heterodimer. Associated live-cell imaging experiments provide a mechanism for Ctf3c and Cnn1-Wip1 recruitment to the kinetochore. The mechanism suggests feedback regulation of Ctf19c assembly and unanticipated similarities in kinetochore organization between yeast and vertebrates.
    MeSH term(s) Anaphase ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Kinetochores/metabolism ; Microtubules/metabolism ; Mitosis ; Protein Phosphatase 2C/genetics ; Protein Phosphatase 2C/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Cell Cycle Proteins ; Cnn1 protein, S cerevisiae ; Ctf3 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Protein Phosphatase 2C (EC 3.1.3.16)
    Language English
    Publishing date 2020-07-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2020.06.024
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  6. Article ; Online: Correction

    Stephen M Hinshaw / Stephen C Harrison

    eLife, Vol

    The structure of the Ctf19c/CCAN from budding yeast

    2020  Volume 9

    Keywords Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-03-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
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  7. Article: The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca

    De Sautu, Marilina / Herrmann, Tobias / Jenni, Simon / Harrison, Stephen C

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Rotaviruses infect cells by delivering into the cytosol a transcriptionally active inner capsid particle (a "double-layer particle": DLP). Delivery is the function of a third, outer layer, which drives uptake from the cell surface into small vesicles ... ...

    Abstract Rotaviruses infect cells by delivering into the cytosol a transcriptionally active inner capsid particle (a "double-layer particle": DLP). Delivery is the function of a third, outer layer, which drives uptake from the cell surface into small vesicles from which the DLPs escape. In published work, we followed stages of rhesus rotavirus (RRV) entry by live-cell imaging and correlated them with structures from cryogenic electron microscopy and tomography (cryo-EM and cryo-ET). The virus appears to wrap itself in membrane, leading to complete engulfment and loss of Ca
    Language English
    Publishing date 2023-10-16
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.10.15.562449
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  8. Article ; Online: The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.

    de Sautu, Marilina / Herrmann, Tobias / Scanavachi, Gustavo / Jenni, Simon / Harrison, Stephen C

    PLoS pathogens

    2024  Volume 20, Issue 4, Page(s) e1011750

    Abstract: ... that viral fusion proteins undergo to penetrate a membrane. The rearrangement of VP5* thrusts a 250-residue, C-terminal ... single-particle fluorescence imaging of liposome-attached TLPs, we confirm insertion of the VP4 C ...

    Abstract Rotaviruses infect cells by delivering into the cytosol a transcriptionally active inner capsid particle (a "double-layer particle": DLP). Delivery is the function of a third, outer layer, which drives uptake from the cell surface into small vesicles from which the DLPs escape. In published work, we followed stages of rhesus rotavirus (RRV) entry by live-cell imaging and correlated them with structures from cryogenic electron microscopy and tomography (cryo-EM and cryo-ET). The virus appears to wrap itself in membrane, leading to complete engulfment and loss of Ca2+ from the vesicle produced by the wrapping. One of the outer-layer proteins, VP7, is a Ca2+-stabilized trimer; loss of Ca2+ releases both VP7 and the other outer-layer protein, VP4, from the particle. VP4, activated by cleavage into VP8* and VP5*, is a trimer that undergoes a large-scale conformational rearrangement, reminiscent of the transition that viral fusion proteins undergo to penetrate a membrane. The rearrangement of VP5* thrusts a 250-residue, C-terminal segment of each of the three subunits outward, while allowing the protein to remain attached to the virus particle and to the cell being infected. We proposed that this segment inserts into the membrane of the target cell, enabling Ca2+ to cross. In the work reported here, we show the validity of key aspects of this proposed sequence. By cryo-EM studies of liposome-attached virions ("triple-layer particles": TLPs) and single-particle fluorescence imaging of liposome-attached TLPs, we confirm insertion of the VP4 C-terminal segment into the membrane and ensuing generation of a Ca2+ "leak". The results allow us to formulate a molecular description of early events in entry. We also discuss our observations in the context of other work on double-strand RNA virus entry.
    MeSH term(s) Rotavirus/genetics ; Capsid Proteins/metabolism ; Capsid/metabolism ; Calcium/metabolism ; Liposomes/analysis ; Liposomes/metabolism
    Chemical Substances Capsid Proteins ; Calcium (SY7Q814VUP) ; Liposomes
    Language English
    Publishing date 2024-04-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011750
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  9. Article ; Online: Recognition of centromere-specific histone Cse4 by the inner kinetochore Okp1-Ame1 complex.

    Deng, Sunbin / Cai, Jiaxi / Harrison, Stephen C / Zhou, Huilin / Hinshaw, Stephen M

    EMBO reports

    2023  Volume 24, Issue 12, Page(s) e57702

    Abstract: Successful mitosis depends on the timely establishment of correct chromosomal attachments to microtubules. The kinetochore, a modular multiprotein complex, mediates this connection by recognizing specialized chromatin containing a histone H3 variant ... ...

    Abstract Successful mitosis depends on the timely establishment of correct chromosomal attachments to microtubules. The kinetochore, a modular multiprotein complex, mediates this connection by recognizing specialized chromatin containing a histone H3 variant called Cse4 in budding yeast and CENP-A in vertebrates. Structural features of the kinetochore that enable discrimination between Cse4/CENP-A and H3 have been identified in several species. How and when these contribute to centromere recognition and how they relate to the overall structure of the inner kinetochore are unsettled questions. More generally, this molecular recognition ensures that only one kinetochore is built on each chromatid and that this happens at the right place on the chromatin fiber. We have determined the crystal structure of a Cse4 peptide bound to the essential inner kinetochore Okp1-Ame1 heterodimer from budding yeast. The structure and related experiments show in detail an essential point of Cse4 contact and provide information about the arrangement of the inner kinetochore.
    MeSH term(s) Cell Cycle Proteins/metabolism ; Centromere/metabolism ; Centromere Protein A/metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; DNA-Binding Proteins/genetics ; Histones/metabolism ; Kinetochores/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomycetales/metabolism
    Chemical Substances Cell Cycle Proteins ; Centromere Protein A ; Chromatin ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Histones ; Saccharomyces cerevisiae Proteins ; CSE4 protein, S cerevisiae ; Okp1 protein, S cerevisiae ; Ame1 protein, S cerevisiae
    Language English
    Publishing date 2023-11-20
    Publishing country England
    Document type Journal Article
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.202357702
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  10. Article ; Online: The human dimension in contemporary biological research.

    Mancia, Filippo / Harrison, Stephen C

    Nature structural & molecular biology

    2020  Volume 27, Issue 2, Page(s) 107–108

    MeSH term(s) Animals ; Cryoelectron Microscopy ; Crystallography, X-Ray ; History, 20th Century ; History, 21st Century ; Interpersonal Relations ; Nucleic Acids/chemistry ; Proteins/chemistry ; Research
    Chemical Substances Nucleic Acids ; Proteins
    Language English
    Publishing date 2020-01-28
    Publishing country United States
    Document type Biography ; Festschrift ; Historical Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-020-0377-9
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