Publikation:

Characterization of the ubiquitin-associated domain of αNAC

Lade...
Vorschaubild

Dateien

Ulusoy_2-k1eo5t0gh3yq7.pdf
Ulusoy_2-k1eo5t0gh3yq7.pdfGröße: 8.93 MBDownloads: 27

Datum

2022

Autor:innen

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

DOI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Dissertation
Publikationsstatus
Published

Erschienen in

Zusammenfassung

Protein biogenesis in cells is carried out by cytosolic ribosomes, which translate proteins from all cellular compartments, including the cytosol, mitochondria, and endoplasmic reticulum (ER). While cytosolic proteins must be folded directly, mitochondrial and ER proteins must first be transported to the corresponding cell organelle to become functionally active. The newly synthesized proteins are co-translationally sorted into the correct biogenesis pathway by ribosome-associated factors that bind to the tunnel exit of the ribosome, where the nascent chains are released into the cytosol. The first factor that interacts with translated proteins in eukaryotes is the nascent polypeptide-associated complex (NAC), a heterodimeric complex consisting of an α and β subunit (αNAC and βNAC). NAC is an essential factor that prevents the ER targeting factor signal recognition particle (SRP) from binding nonspecifically to ribosomes that translate mitochondrial or cytosolic substrates to prevent mislocalization of proteins in cells. The mechanism of how NAC inhibits the ER targeting machinery and how this inhibition is overcome on ribosomes translating ER proteins is unknown. The main objective of the present work was to gain a deeper understanding of the interaction mechanism of NAC with ribosomes and other co-translational protein biogenesis factors. Focus was placed on a conserved structured domain, the ubiquitin-associated domain (UBA),

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

NAC, SRP, UBA, Protein targeting

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690ULUSOY, Zeynel, 2022. Characterization of the ubiquitin-associated domain of αNAC [Dissertation]. Konstanz: Universität Konstanz
BibTex
@phdthesis{Ulusoy2022Chara-57861,
  year={2022},
  title={Characterization of the ubiquitin-associated domain of αNAC},
  author={Ulusoy, Zeynel},
  address={Konstanz},
  school={Universität Konstanz}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/57861">
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-06-29T10:31:27Z</dc:date>
    <dcterms:title>Characterization of the ubiquitin-associated domain of αNAC</dcterms:title>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:creator>Ulusoy, Zeynel</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:issued>2022</dcterms:issued>
    <dc:contributor>Ulusoy, Zeynel</dc:contributor>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/57861/3/Ulusoy_2-k1eo5t0gh3yq7.pdf"/>
    <dc:rights>terms-of-use</dc:rights>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/57861"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-06-29T10:31:27Z</dcterms:available>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/57861/3/Ulusoy_2-k1eo5t0gh3yq7.pdf"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:language>eng</dc:language>
    <dcterms:abstract xml:lang="eng">Protein biogenesis in cells is carried out by cytosolic ribosomes, which translate proteins from all cellular compartments, including the cytosol, mitochondria, and endoplasmic reticulum (ER). While cytosolic proteins must be folded directly, mitochondrial and ER proteins must first be transported to the corresponding cell organelle to become functionally active. The newly synthesized proteins are co-translationally sorted into the correct biogenesis pathway by ribosome-associated factors that bind to the tunnel exit of the ribosome, where the nascent chains are released into the cytosol. The first factor that interacts with translated proteins in eukaryotes is the nascent polypeptide-associated complex (NAC), a heterodimeric complex consisting of an α and β subunit (αNAC and βNAC). NAC is an essential factor that prevents the ER targeting factor signal recognition particle (SRP) from binding nonspecifically to ribosomes that translate mitochondrial or cytosolic substrates to prevent mislocalization of proteins in cells. The mechanism of how NAC inhibits the ER targeting machinery and how this inhibition is overcome on ribosomes translating ER proteins is unknown. The main objective of the present work was to gain a deeper understanding of the interaction mechanism of NAC with ribosomes and other co-translational protein biogenesis factors. Focus was placed on a conserved structured domain, the ubiquitin-associated domain (UBA),</dcterms:abstract>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

May 31, 2022
Hochschulschriftenvermerk
Konstanz, Univ., Diss., 2022
Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen