Evidence map›Paper›PMID 14517307›Full record

ArticleMolecular and cellular biology2003

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

Matthias Gautschi, Sören Just, Andrej Mun, Suzanne Ross, Peter Rücknagel, Yves Dubaquié, Ann Ehrenhofer-Murray, Sabine Rospert

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In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
4.9field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

130 citing papers in PubMed, 226 citations in OpenAlex.

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70 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Matthias GautschiMax Planck Research Unit Enzymology of Protein Folding, D-06120 Halle, Germany.
Sören Just
Andrej Mun
Suzanne Ross
Peter Rücknagel
Yves Dubaquié
Ann Ehrenhofer-Murray
Sabine Rospert
Max Planck Research Unit for Enzymology of Protein Folding · DEBristol-Myers Squibb (United States) · USMax Planck Institute for Molecular Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The majority of cytosolic proteins in eukaryotes contain a covalently linked acetyl moiety at their very N terminus. The mechanism by which the acetyl moiety is efficiently transferred to a large variety of nascent polypeptides is currently only poorly understood. Yeast N(alpha)-acetyltransferase NatA, consisting of the known subunits Nat1p and the catalytically active Ard1p, recognizes a wide range of sequences and is thought to act cotranslationally. We found that NatA was quantitatively bound to ribosomes via Nat1p and contained a previously unrecognized third subunit, the N(alpha)-acetyltransferase homologue Nat5p. Nat1p not only anchored Ard1p and Nat5p to the ribosome but also was in close proximity to nascent polypeptides, independent of whether they were substrates for N(alpha)-acetylation or not. Besides Nat1p, NAC (nascent polypeptide-associated complex) and the Hsp70 homologue Ssb1/2p interact with a variety of nascent polypeptides on the yeast ribosome. A direct comparison revealed that Nat1p required longer nascent polypeptides for interaction than NAC and Ssb1/2p. Delta nat1 or Delta ard1 deletion strains were temperature sensitive and showed derepression of silent mating type loci while Delta nat5 did not display any obvious phenotype. Temperature sensitivity and derepression of silent mating type loci caused by Delta nat1 or Delta ard1 were partially suppressed by overexpression of SSB1. The combination of data suggests that Nat1p presents the N termini of nascent polypeptides for acetylation and might serve additional roles during protein synthesis.

Indexed as

AcetyltransferasesAmino AcidsAmino Acid SequenceCatalysisCross-Linking ReagentsCytosolFungal ProteinsHSP70 Heat-Shock ProteinsModels, BiologicalMolecular Sequence DataN-Terminal Acetyltransferase APeptidesPhenotypePlasmidsPrecipitin TestsProtein BindingAcetyltransferasesAmino AcidsARD1 protein, S cerevisiaeCross-Linking ReagentsFungal ProteinsHSP70 Heat-Shock ProteinsNAT1 protein, S cerevisiaeN-Terminal Acetyltransferase APeptidesprotein N-terminal acetyltransferaseSaccharomyces cerevisiae Proteins

Identifiers

PMID14517307
PMCPMC230319
OpenAlexW2004500138

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.