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  1. Artikel ; Online: Structure of mitotic chromosomes.

    Beel, Andrew J / Azubel, Maia / Matteï, Pierre-Jean / Kornberg, Roger D

    Molecular cell

    2021  Band 81, Heft 21, Seite(n) 4369–4376.e3

    Abstract: Chromatin fibers must fold or coil in the process of chromosome condensation. Patterns of coiling have been demonstrated for reconstituted chromatin, but the actual trajectories of fibers in condensed states of chromosomes could not be visualized because ...

    Abstract Chromatin fibers must fold or coil in the process of chromosome condensation. Patterns of coiling have been demonstrated for reconstituted chromatin, but the actual trajectories of fibers in condensed states of chromosomes could not be visualized because of the high density of the material. We have exploited partial decondensation of mitotic chromosomes to reveal their internal structure at sub-nucleosomal resolution by cryo-electron tomography, without the use of stains, fixatives, milling, or sectioning. DNA gyres around nucleosomes were visible, allowing the nucleosomes to be identified and their orientations to be determined. Linker DNA regions were traced, revealing the trajectories of the chromatin fibers. The trajectories were irregular, with almost no evidence of coiling and no short- or long-range order of the chromosomal material. The 146-bp core particle, long known as a product of nuclease digestion, is identified as the native state of the nucleosome, with no regular spacing along the chromatin fibers.
    Mesh-Begriff(e) Amino Acid Motifs ; Chromatin/chemistry ; Chromosomes/ultrastructure ; Cryoelectron Microscopy ; DNA/chemistry ; Green Fluorescent Proteins/metabolism ; HeLa Cells ; Histones/chemistry ; Humans ; Microscopy, Fluorescence ; Mitosis ; Nucleosomes/chemistry ; Nucleosomes/metabolism ; Spermidine/chemistry ; Tomography
    Chemische Substanzen Chromatin ; Histones ; Nucleosomes ; Green Fluorescent Proteins (147336-22-9) ; DNA (9007-49-2) ; Spermidine (U87FK77H25)
    Sprache Englisch
    Erscheinungsdatum 2021-09-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.08.020
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Structure of mitotic chromosomes

    Beel, Andrew J. / Azubel, Maia / Matteï, Pierre-Jean / Kornberg, Roger D.

    Molecular cell. 2021 Nov. 04, v. 81, no. 21

    2021  

    Abstract: Chromatin fibers must fold or coil in the process of chromosome condensation. Patterns of coiling have been demonstrated for reconstituted chromatin, but the actual trajectories of fibers in condensed states of chromosomes could not be visualized because ...

    Abstract Chromatin fibers must fold or coil in the process of chromosome condensation. Patterns of coiling have been demonstrated for reconstituted chromatin, but the actual trajectories of fibers in condensed states of chromosomes could not be visualized because of the high density of the material. We have exploited partial decondensation of mitotic chromosomes to reveal their internal structure at sub-nucleosomal resolution by cryo-electron tomography, without the use of stains, fixatives, milling, or sectioning. DNA gyres around nucleosomes were visible, allowing the nucleosomes to be identified and their orientations to be determined. Linker DNA regions were traced, revealing the trajectories of the chromatin fibers. The trajectories were irregular, with almost no evidence of coiling and no short- or long-range order of the chromosomal material. The 146-bp core particle, long known as a product of nuclease digestion, is identified as the native state of the nucleosome, with no regular spacing along the chromatin fibers.
    Schlagwörter DNA ; chromosome morphology ; mitosis ; nucleosomes ; tomography
    Sprache Englisch
    Erscheinungsverlauf 2021-1104
    Umfang p. 4369-4376.e3.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.08.020
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  3. Artikel ; Online: Bridging cell wall biosynthesis and bacterial morphogenesis.

    Matteï, Pierre-Jean / Neves, David / Dessen, Andréa

    Current opinion in structural biology

    2010  Band 20, Heft 6, Seite(n) 749–755

    Abstract: The bacterial cell wall is a complex three-dimensional structure that protects the cell from environmental stress and ensures its shape. The biosynthesis of its main component, the peptidoglycan, involves the coordination of activities of proteins ... ...

    Abstract The bacterial cell wall is a complex three-dimensional structure that protects the cell from environmental stress and ensures its shape. The biosynthesis of its main component, the peptidoglycan, involves the coordination of activities of proteins present in the cytoplasm, the membrane, and the periplasm, some of which also interact with the bacterial cytoskeleton. The sheer complexity of the cell wall elongation process, which is the main focus of this review, has created a significant challenge for the study of the macromolecular interactions that regulate peptidoglycan biosynthesis. The availability of new structural and biochemical data on a number of components of peptidoglycan assembly machineries, including a complex between MreB and RodZ as well as structures of penicillin-binding proteins (PBPs) from a number of pathogenic species, now provide novel insight into the underpinnings of an intricate molecular machinery.
    Mesh-Begriff(e) Bacteria/cytology ; Bacteria/growth & development ; Bacteria/metabolism ; Bacterial Proteins/metabolism ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cell Wall/metabolism ; Cytoplasm/metabolism ; Morphogenesis
    Chemische Substanzen Bacterial Proteins
    Sprache Englisch
    Erscheinungsdatum 2010-12
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2010.09.014
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  4. Artikel ; Online: Ultra-high field magnetic resonance imaging of the quadriceps tendon enthesis in healthy subjects.

    Guenoun, Daphne / Wirth, Theo / Roche, Damien / Michel, Constance P / Daudé, Pierre / Ogier, Augustin C / Chagnaud, Christophe / Mattei, Jean Pierre / Pini, Lauriane / Guye, Maxime / Ollivier, Matthieu / Bendahan, David / Guis, Sandrine

    Surgical and radiologic anatomy : SRA

    2023  Band 45, Heft 8, Seite(n) 1049–1054

    Abstract: Purpose: Although enthesitis is a hallmark of several rheumatologic conditions, current imaging methods are still unable to characterize entheses changes because of the corresponding short transverse relaxation times (T2). A growing number of MR studies ...

    Abstract Purpose: Although enthesitis is a hallmark of several rheumatologic conditions, current imaging methods are still unable to characterize entheses changes because of the corresponding short transverse relaxation times (T2). A growing number of MR studies have used Ultra-High Field (UHF) MRI in order to assess low-T2 tissues e.g., tendon but never in humans. The purpose of the present study was to assess in vivo the enthesis of the quadriceps tendon in healthy subjects using UHF MRI.
    Methods: Eleven healthy subjects volunteered in an osteoarthritis imaging study. The inclusion criteria were: no knee trauma, Lequesne index = 0, less than 3 h of sport activities per week, and Kellgren and Lawrence grade = 0. 3D MR images were acquired at 7 T using GRE sequences and a T2* mapping. Regions of interest i.e., trabecular bone, subchondral bone, enthesis, and tendon body were identified, and T2* values were quantified and compared.
    Results: Quadriceps tendon enthesis was visible as a hyper-intense signal. The largest and the lowest T2* values were quantified in the subchondral bone region and the tendon body respectively. T2* value within subchondral bone was significantly higher than T2* value within the enthesis. T2* in subchondral bone region was significantly higher than the whole tendon body T2*.
    Conclusion: A T2* gradient was observed along the axis from the enthesis toward the tendon body. It illustrates different water biophysical properties. These results provide normative values which could be used in the field of inflammatory rheumatologic diseases and mechanical disorders affecting the tendon.
    Mesh-Begriff(e) Humans ; Healthy Volunteers ; Tendons/diagnostic imaging ; Imaging, Three-Dimensional/methods ; Magnetic Resonance Imaging/methods ; Arthritis, Rheumatoid
    Sprache Englisch
    Erscheinungsdatum 2023-06-05
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ZDB-ID 632839-8
    ISSN 1279-8517 ; 0930-312X ; 0930-1038
    ISSN (online) 1279-8517
    ISSN 0930-312X ; 0930-1038
    DOI 10.1007/s00276-023-03175-y
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  5. Artikel ; Online: Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex

    Carlos Contreras-Martel / Alexandre Martins / Chantal Ecobichon / Daniel Maragno Trindade / Pierre-Jean Matteï / Samia Hicham / Pierre Hardouin / Meriem El Ghachi / Ivo G. Boneca / Andréa Dessen

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Band 10

    Abstract: Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its ... ...

    Abstract Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth.
    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2017-10-01T00:00:00Z
    Verlag Nature Publishing Group
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  6. Artikel ; Online: Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex

    Carlos Contreras-Martel / Alexandre Martins / Chantal Ecobichon / Daniel Maragno Trindade / Pierre-Jean Matteï / Samia Hicham / Pierre Hardouin / Meriem El Ghachi / Ivo G. Boneca / Andréa Dessen

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Band 10

    Abstract: Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its ... ...

    Abstract Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth.
    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2017-10-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  7. Artikel: Improved Metastatic-Free Survival after Systematic Re-Excision Following Complete Macroscopic Unplanned Excision of Limb or Trunk Soft Tissue Sarcoma.

    Gouin, Francois / Michot, Audrey / Jafari, Mehrdad / Honoré, Charles / Mattei, Jean Camille / Rochwerger, Alexandre / Ropars, Mickael / Tzanis, Dimitri / Anract, Philippe / Carrere, Sébastien / Gangloff, Dimitri / Ducoulombier, Agnès / Lebbe, Céleste / Guiramand, Jérôme / Waast, Denis / Marchal, Frédéric / Sirveaux, François / Causeret, Sylvain / Gimbergues, Pierre /
    Fiorenza, Fabrice / Paquette, Brice / Soibinet, Pauline / Guilloit, Jean-Marc / Le Nail, Louis R / Dujardin, Franck / Brinkert, David / Chemin-Airiau, Claire / Morelle, Magali / Meeus, Pierre / Karanian, Marie / Le Loarer, François / Vaz, Gualter / Blay, Jean-Yves

    Cancers

    2024  Band 16, Heft 7

    Abstract: Background: Whether re-excision (RE) of a soft tissue sarcoma (STS) of limb or trunk should be systematized as adjuvant care and if it would improve metastatic free survival (MFS) are still debated. The impact of resection margins after unplanned ... ...

    Abstract Background: Whether re-excision (RE) of a soft tissue sarcoma (STS) of limb or trunk should be systematized as adjuvant care and if it would improve metastatic free survival (MFS) are still debated. The impact of resection margins after unplanned macroscopically complete excision (UE) performed out of a NETSARC reference center or after second resection was further investigated.
    Methods: This large nationwide series used data from patients having experienced UE outside of a reference center from 2010 to 2019, collected in a French nationwide exhaustive prospective cohort NETSARC. Patient characteristics and survival distributions in patients reexcised (RE) or not (No-RE) are reported. Multivariate Cox proportional hazard model was conducted to adjust for classical prognosis factors. Subgroup analysis were performed to identify which patients may benefit from RE.
    Results: Out of 2371 patients with UE for STS performed outside NETSARC reference centers, 1692 patients were not reviewed by multidisciplinary board before treatment decision and had a second operation documented. Among them, 913 patients experienced re-excision, and 779 were not re-excised. Characteristics were significantly different regarding patient age, tumor site, size, depth, grade and histotype in patients re-excised (RE) or not (No-RE). In univariate analysis, final R0 margins are associated with a better MFS, patients with R1 margins documented at first surgery had a better MFS as compared to patients with first R0 resection. The study identified RE as an independent favorable factor for MFS (HR 0.7, 95% CI 0.53-0.93;
    Conclusions: RE might be considered in patients with STS of limb or trunk, with UE with macroscopic complete resection performed out of a reference center, and also in originally defined R0 margin resections, to improve LRFS and MFS. Systematic RE should not be advocated for patients older than 70 years, or with tumors greater than 10 cm.
    Sprache Englisch
    Erscheinungsdatum 2024-03-30
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers16071365
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  8. Artikel ; Online: Uncoupling Promoter Opening from Start-Site Scanning.

    Murakami, Kenji / Mattei, Pierre-Jean / Davis, Ralph E / Jin, Huiyan / Kaplan, Craig D / Kornberg, Roger D

    Molecular cell

    2015  Band 59, Heft 1, Seite(n) 133–138

    Abstract: Whereas RNA polymerase II (Pol II) transcription start sites (TSSs) occur about 30-35 bp downstream of the TATA box in metazoans, TSSs are located 40-120 bp downstream in S. cerevisiae. Promoter melting begins about 12 bp downstream in all eukaryotes, so ...

    Abstract Whereas RNA polymerase II (Pol II) transcription start sites (TSSs) occur about 30-35 bp downstream of the TATA box in metazoans, TSSs are located 40-120 bp downstream in S. cerevisiae. Promoter melting begins about 12 bp downstream in all eukaryotes, so Pol II is presumed to "scan" further downstream before starting transcription in yeast. Here we report that removal of the kinase complex TFIIK from TFIIH shifts the TSS in a yeast system upstream to the location observed in metazoans. Conversely, moving the normal TSS to an upstream location enables a high level of TFIIK-independent transcription in the yeast system. We distinguish two stages of the transcription initiation process: bubble formation by TFIIH, which fills the Pol II active center with single-stranded DNA, and subsequent scanning downstream, also driven by TFIIH, which requires displacement of the initial bubble. Omission of TFIIK uncouples the two stages of the process.
    Mesh-Begriff(e) Base Sequence ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; RNA Polymerase II/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription Factor TFIIH/genetics ; Transcription Factor TFIIH/metabolism ; Transcription Initiation Site/physiology ; Transcription, Genetic/genetics
    Chemische Substanzen Saccharomyces cerevisiae Proteins ; Transcription Factor TFIIH (148710-81-0) ; RNA Polymerase II (EC 2.7.7.-)
    Sprache Englisch
    Erscheinungsdatum 2015-07-02
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2015.05.021
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  9. Artikel ; Online: Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.

    Contreras-Martel, Carlos / Martins, Alexandre / Ecobichon, Chantal / Trindade, Daniel Maragno / Matteï, Pierre-Jean / Hicham, Samia / Hardouin, Pierre / Ghachi, Meriem El / Boneca, Ivo G / Dessen, Andréa

    Nature communications

    2017  Band 8, Heft 1, Seite(n) 776

    Abstract: Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the "divisome") and lateral wall growth (the "elongasome"). ... ...

    Abstract Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the "divisome") and lateral wall growth (the "elongasome"). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2:MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2:MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors.Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth.
    Mesh-Begriff(e) Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Binding Sites ; Cell Wall/metabolism ; Crystallography, X-Ray ; Helicobacter pylori/genetics ; Helicobacter pylori/metabolism ; Models, Molecular ; Penicillin-Binding Proteins/chemistry ; Penicillin-Binding Proteins/genetics ; Protein Structure, Tertiary ; Sequence Alignment
    Chemische Substanzen Bacterial Proteins ; MreC protein, Bacteria ; Penicillin-Binding Proteins
    Sprache Englisch
    Erscheinungsdatum 2017-10-03
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2041-1723
    ISSN (online) 2041-1723
    DOI 10.1038/s41467-017-00783-2
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel: Membrane targeting and pore formation by the type III secretion system translocon

    Matteï, Pierre-Jean / Faudry, Eric / Job, Viviana / Izoré, Thierry / Attree, Ina / Dessen, Andréa

    FEBS journal. 2011 Feb., v. 278, no. 3

    2011  

    Abstract: The type III secretion system (T3SS) is a complex macromolecular machinery employed by a number of Gram-negative species to initiate infection. Toxins secreted through the system are synthesized in the bacterial cytoplasm and utilize the T3SS to pass ... ...

    Abstract The type III secretion system (T3SS) is a complex macromolecular machinery employed by a number of Gram-negative species to initiate infection. Toxins secreted through the system are synthesized in the bacterial cytoplasm and utilize the T3SS to pass through both bacterial membranes and the periplasm, thus being introduced directly into the eukaryotic cytoplasm. A key element of the T3SS of all bacterial pathogens is the translocon, which comprises a pore that is inserted into the membrane of the target cell, allowing toxin injection. Three macromolecular partners associate to form the translocon: two are hydrophobic and one is hydrophilic, and the latter also associates with the T3SS needle. In this review, we discuss recent advances on the biochemical and structural characterization of the proteins involved in translocon formation, as well as their participation in the modification of intracellular signalling pathways upon infection. Models of translocon assembly and regulation are also discussed.
    Sprache Englisch
    Erscheinungsverlauf 2011-02
    Umfang p. 414-426.
    Erscheinungsort Blackwell Publishing Ltd
    Dokumenttyp Artikel
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/j.1742-4658.2010.07974.x
    Datenquelle NAL Katalog (AGRICOLA)

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