Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Feb 9;128(8):1156–1169. doi: 10.1161/CIRCRESAHA.120.316966

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2021 The Authors.

Circulation Research is published on behalf of the American Heart Association, Inc., by Wolters Kluwer Health, Inc. This is an open access article under the terms of the Creative Commons Attribution Non-Commercial-NoDerivs License, which permits use, distribution, and reproduction in any medium, provided that the original work is properly cited, the use is noncommercial, and no modifications or adaptations are made.

This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

PMC Copyright notice

Figure 3. — N-terminal acetylation in NAA15^+/− and NAA15^−/− induced pluripotent stem cells (iPSCs). A, N-terminal peptides acetylated in NAA15^+/+ iPSCs are categorized by NAT-type substrate specificity. NatA (N-terminal acetyltransferase) targets are displayed according to percent Nt-acetylation; Nt-acetylation >10% highlighted in gold and Nt-acetylation <10% highlighted in light gold. B and C, The number of Nt-acetylated NatA-type N-terminal peptides represented by residues A, G, S, T, or V in NAA15 mutant and wildtype iPSCs. Data is displayed as the absolute number of peptides measured from the sum of 2 biological replicates for each genotype. Alanine and serine residues are preferentially acetylated in peptides with >10% Nt-acetylation; glycine and valine residues are representative of N-termini with <10% Nt-acetylation. Primary peptide summary provided in Table V in the Data Supplement. There were no statistically significant differences between genotypes (hypergeometric test; data not shown). D–F, Representative scatter plots display the correlation of the degrees of Nt-acetylation of all N-termini identified as NatA targets in NAA15^−/−, NAA15^+/−, NAA15^+/R276W, and NAA15^+/+ iPSCs. Each plot compares NAA15 (N-alpha-acetyltransferase 15) mutant iPSCs to wildtype iPSCs. Differentially acetylated N-termini are found below the line of identity (y intercept=0, slope=1). Peptides lose acetylation moieties in NAA15-mutant iPSCs. NAA15^−/− iPSCs have the largest number of peptides (n=32) with reduced Nt-acetylation. There are N-termini with reduced N-terminal acetylation in NAA15^+/− iPSCs (n=9) and NAA15^+/R276W iPSCs (n=8). Decreased protein expression changes are highlighted in red. COPS3 indicates COP9 signalosome complex subunit 3; DDX54, ATP-dependent RNA helicase; NDUFB6, NADH dehydrogenase (ubiquinone) 1β subcomplex subunit 6; PABPN1, polyadenylate-binding protein 2; PPWD1, peptidyl-prolyl isomerase domain and WD repeat-containing protein 1; and VPS4A, vacuolar protein sorting-associated protein 4.