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Verfasst von:Manalastas-Cantos, Karen [VerfasserIn]   i
 Kschonsak, Marc [VerfasserIn]   i
 Häring, Christian [VerfasserIn]   i
 Svergun, Dmitri I. [VerfasserIn]   i
Titel:Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1
Verf.angabe:Karen Manalastas-Cantos, Marc Kschonsak, Christian H. Haering, and Dmitri I. Svergun
E-Jahr:2019
Jahr:July 26, 2019
Umfang:8 S.
Fussnoten:Gesehen am 27.02.2020
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : Soc., 1905
Jahr Quelle:2019
Band/Heft Quelle:294(2019), 37, Seite 13822-13829
ISSN Quelle:1083-351X
Abstract:High-resolution structural analysis of flexible proteins is frequently challenging and requires the synergistic application of different experimental techniques. For these proteins, small-angle X-ray scattering (SAXS) allows for a quantitative assessment and modeling of potentially flexible and heterogeneous structural states. Here, we report SAXS characterization of the condensin HEAT-repeat subunit Ycg1Cnd3 in solution, complementing currently available high-resolution crystallographic models. We show that the free Ycg1 subunit is flexible in solution but becomes considerably more rigid when bound to its kleisin-binding partner protein Brn1Cnd2 The analysis of SAXS and dynamic and static multiangle light scattering data furthermore reveals that Ycg1 tends to oligomerize with increasing concentrations in the absence of Brn1. Based on these data, we present a model of the free Ycg1 protein constructed by normal mode analysis, as well as tentative models of Ycg1 dimers and tetramers. These models enable visualization of the conformational transitions that Ycg1 has to undergo to adopt a closed rigid shape and thereby create a DNA-binding surface in the condensin complex.
DOI:doi:10.1074/jbc.RA119.008661
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: http://dx.doi.org/10.1074/jbc.RA119.008661
 DOI: https://doi.org/10.1074/jbc.RA119.008661
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:condensin
 conformational change
 DNA binding protein
 dynamic light scattering (DLS)
 HEAT-repeat
 oligomer
 protein flexibility
 size exclusion chromatography with multiangle static light scattering (SEC-MALS)
 small-angle X-ray scattering (SAXS)
 structural model
K10plus-PPN:169116237X
Verknüpfungen:→ Zeitschrift

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