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A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel
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Yeast Nα-terminal acetyltransferases are associated with ribosomes
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N-terminal ubiquitination: more protein substrates join in
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The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway
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The tumor suppressor protein p16INK4a and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system -: Direct evidence for ubiquitination at the N-terminal residue
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Golgi targeting of ARF-like GTPase Arl3p requires its Nα-acetylation and the integral membrane protein Sys1p
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Targeting of the arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p
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The yeast Nα-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
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MOLECULAR AND CELLULAR BIOLOGY (2003)
Nat3p and Mdm20p are required for function of yeast NatB Nα-terminal acetyltransferase and of actin and tropomyosin
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Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast
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