Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Becker, Matthias Michael Markus [VerfasserIn]   i
 Lapouge, Karine [VerfasserIn]   i
 Segnitz, Bernd [VerfasserIn]   i
 Wild, Klemens [VerfasserIn]   i
 Sinning, Irmgard [VerfasserIn]   i
Titel:Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction
Verf.angabe:Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning
Jahr:2017
Umfang:12 S.
Fussnoten:Published online 28 November 2016 ; Gesehen am 11.09.2018
Titel Quelle:Enthalten in: Nucleic acids research
Ort Quelle:Oxford : Oxford Univ. Press, 1974
Jahr Quelle:2017
Band/Heft Quelle:45(2017), 1, Seite 470-481
ISSN Quelle:1362-4962
Abstract:Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K+-turn. In addition, SRP72-RBD remodels the 5f-loop involved in ribosome binding and visualizes SRP RNA plasticity. Docking of the S domain structure into cryo-electron microscopy density maps reveals multiple contact sites between SRP68/72 and the ribosome, and explains the role of SRP72 in the SRP pathway.
DOI:doi:10.1093/nar/gkw1124
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.

kostenfrei: Volltext: http://dx.doi.org/10.1093/nar/gkw1124
 kostenfrei: Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5224484/
 DOI: https://doi.org/10.1093/nar/gkw1124
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1580844391
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/68303806   QR-Code
zum Seitenanfang