Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo.

FEBS letters - 10 Apr 2002

George Rebecca, Walsh Peter, Beddoe Travis, Lithgow Trevor

Abstract excerpt

The nascent polypeptide-associated complex (NAC) is a peripheral component of cytoplasmic ribosomes, and interacts with nascent chains as they leave the ribosome. Yeast mutants lacking NAC translate polypeptides normally, but have fewer ribosomes associated with the mitochondrial surface. The mutants lacking NAC suffer mitochondrial defects and have decreased levels of proteins like fumarase, normally targeted to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biological Transport, Active
Share to Genes, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondria

Share to Molecular Chaperones

Share to Protein Biosynthesis

Share to Ribosomes

Share to Saccharomyces cerevisiae Proteins

Share to Trans-Activators

Source

Identifiers

PMID: 11959135
DOI: 10.1016/s0014-5793(02)02528-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo.PMID 11959135Read ↗

A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.Semantic proximity Read ↗

A molecular switch in NAC prevents mitochondrial protein mistargeting by SRPSemantic proximity Read ↗

Characterisation of the nascent polypeptide-associated complex in fission yeast.Semantic proximity Read ↗

A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes.Semantic proximity Read ↗

Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related ProteinopathiesSemantic proximity Read ↗

Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome.Semantic proximity Read ↗

Visualizing formation of the active site in the mitochondrial ribosome.Semantic proximity Read ↗

Molecular genetics of the peptidyl transferase center and the unusual Var1 protein in yeast mitochondrial ribosomes.Semantic proximity Read ↗

Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein importSemantic proximity Read ↗

Ribosome. The complete structure of the 55S mammalian mitochondrial ribosome.Semantic proximity Read ↗

A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains.Semantic proximity Read ↗

The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.