English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The yeast N-alpha-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides

Gautschi, M., Just, S., Mun, A., Ross, S., Rücknagel, P., Dubaquie, Y., et al. (2003). The yeast N-alpha-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Molecular and Cellular Biology, 23(20), 7403-7414. doi:10.1128/MCB.23.20.7403-7414.2003.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8994-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8995-8
Genre: Journal Article
Alternative Title : Mol. Cell. Biol.

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Gautschi, Matthias, Author
Just, Sören, Author
Mun, Andrej, Author
Ross, Suzanne, Author
Rücknagel, Peter, Author
Dubaquie, Yves, Author
Ehrenhofer-Murray, Ann1, Author              
Rospert, Sabine, Author
Affiliations:
1Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433554              

Content

show
hide
Free keywords: -
 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-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-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-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. nat1 or ard1 deletion strains were temperature sensitive and showed derepression of silent mating type loci while nat5 did not display any obvious phenotype. Temperature sensitivity and derepression of silent mating type loci caused by nat1 or 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.

Details

show
hide
Language(s): eng - English
 Dates: 2003-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular and Cellular Biology
  Alternative Title : Mol. Cell. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 23 (20) Sequence Number: - Start / End Page: 7403 - 7414 Identifier: ISSN: 0270-7306