Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation

Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility t...

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Published inMolecular systems biology Vol. 16; no. 7; pp. e9464 - n/a
Main Authors Bienvenut, Willy V, Brünje, Annika, Boyer, Jean‐Baptiste, Mühlenbeck, Jens S, Bernal, Gautier, Lassowskat, Ines, Dian, Cyril, Linster, Eric, Dinh, Trinh V, Koskela, Minna M, Jung, Vincent, Seidel, Julian, Schyrba, Laura K, Ivanauskaite, Aiste, Eirich, Jürgen, Hell, Rüdiger, Schwarzer, Dirk, Mulo, Paula, Wirtz, Markus, Meinnel, Thierry, Giglione, Carmela, Finkemeier, Iris
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.07.2020
EMBO Press
John Wiley and Sons Inc
Springer Nature
Subjects
Acetylation
acetylome
Acetyltransferase
Biochemistry, Molecular Biology
Cellular Biology
Chloroplasts
Complexity
co‐ and post‐translational modifications
Deactivation
EMBO30
EMBO31
EMBO56
Enzymatic activity
Enzymes
Genomes
Genomics
In vivo methods and tests
Inactivation
Life Sciences
Localization
Lysine
Mass spectrometry
Mass spectroscopy
Peptides
Phylogenetics
plastid
Plastids
Prokaryotes
Proteins
Quantitative Methods
quantitative proteomics
Selectivity
Structural Biology
Subcellular Processes
Vegetal Biology
co‐ and post‐translational modifications
plastid
acetylome
acetyltransferase
quantitative proteomics
Post-translational Modifications & Proteolysis
co-and post-translational modifications
Proteomics
quantitative proteomics Subject Categories Plant Biology
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Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5‐related N ‐acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid‐localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo . In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities. Synopsis A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN5‐related N ‐acetyltransferases (GNATs) have unique amino acid sequence characteristics and unambiguously possess dual N ‐α‐ and ε‐lysine acetylation activities. An in silico search for putative plastidial N‐terminal and lysine acetyltransferases reveals 10 putative GNAT candidates, showing unique features both at the level of the conserved motifs and key residues. Localization to chloroplasts is confirmed for seven of them, while another one is either associated to chloroplasts or localized within the nucleus. All plastid‐associated GNATs display distinct lysine acetyltransferase and relaxed N‐ terminal acetyltransferase substrate specificities. Inactivation of GNAT2, the plastid GNAT involved in photosynthetic state transitions, results in NTA decreases confined to chloroplast proteins, next to the known decreases on photosynthetic KA target proteins. Graphical Abstract A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN5‐related N ‐acetyltransferases (GNATs) have unique amino acid sequence characteristics and unambiguously possess dual N ‐α‐ and ε‐lysine acetylation activities.
AbstractList Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5‐related N‐acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid‐localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities.
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5‐related N ‐acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid‐localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo . In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities. Synopsis A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN5‐related N ‐acetyltransferases (GNATs) have unique amino acid sequence characteristics and unambiguously possess dual N ‐α‐ and ε‐lysine acetylation activities. An in silico search for putative plastidial N‐terminal and lysine acetyltransferases reveals 10 putative GNAT candidates, showing unique features both at the level of the conserved motifs and key residues. Localization to chloroplasts is confirmed for seven of them, while another one is either associated to chloroplasts or localized within the nucleus. All plastid‐associated GNATs display distinct lysine acetyltransferase and relaxed N‐ terminal acetyltransferase substrate specificities. Inactivation of GNAT2, the plastid GNAT involved in photosynthetic state transitions, results in NTA decreases confined to chloroplast proteins, next to the known decreases on photosynthetic KA target proteins. Graphical Abstract A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN5‐related N ‐acetyltransferases (GNATs) have unique amino acid sequence characteristics and unambiguously possess dual N ‐α‐ and ε‐lysine acetylation activities.
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-a-acetylation (NTA) and e-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA speci-ficities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzy-matic activities.
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and ε-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities.Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and ε-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities.
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation ( NTA ) and ε‐lysine acetylation ( KA ) are known to be catalyzed by distinct families of enzymes ( NAT s and KAT s, respectively), although the possibility that the same GCN 5‐related N ‐acetyltransferase ( GNAT ) can perform both functions has been debated. Here, we discovered a new family of plastid‐localized GNAT s, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT 2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo . In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNAT s may also possess these previously underappreciated broader enzymatic activities. A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN 5‐related N ‐acetyltransferases ( GNAT s) have unique amino acid sequence characteristics and unambiguously possess dual N ‐α‐ and ε‐lysine acetylation activities.
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5‐related N‐acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid‐localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities. Synopsis A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN5‐related N‐acetyltransferases (GNATs) have unique amino acid sequence characteristics and unambiguously possess dual N‐α‐ and ε‐lysine acetylation activities. An in silico search for putative plastidial N‐terminal and lysine acetyltransferases reveals 10 putative GNAT candidates, showing unique features both at the level of the conserved motifs and key residues. Localization to chloroplasts is confirmed for seven of them, while another one is either associated to chloroplasts or localized within the nucleus. All plastid‐associated GNATs display distinct lysine acetyltransferase and relaxed N‐ terminal acetyltransferase substrate specificities. Inactivation of GNAT2, the plastid GNAT involved in photosynthetic state transitions, results in NTA decreases confined to chloroplast proteins, next to the known decreases on photosynthetic KA target proteins. A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. These GCN5‐related N‐acetyltransferases (GNATs) have unique amino acid sequence characteristics and unambiguously possess dual N‐α‐ and ε‐lysine acetylation activities.
Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5‐related N‐acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid‐localized GNATs, which possess a dual specificity. All characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA specificities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzymatic activities.
Author Koskela, Minna M
Jung, Vincent
Schyrba, Laura K
Linster, Eric
Ivanauskaite, Aiste
Mulo, Paula
Wirtz, Markus
Finkemeier, Iris
Bernal, Gautier
Schwarzer, Dirk
Hell, Rüdiger
Lassowskat, Ines
Brünje, Annika
Dinh, Trinh V
Mühlenbeck, Jens S
Seidel, Julian
Bienvenut, Willy V
Eirich, Jürgen
Dian, Cyril
Meinnel, Thierry
Boyer, Jean‐Baptiste
Giglione, Carmela
AuthorAffiliation 6 Present address: Génétique Quantitative et Évolution Gif‐sur‐Yvette France
2 Plant Physiology Institute of Plant Biology and Biotechnology University of Muenster Muenster Germany
7 Present address: Institute of Plant Sciences Paris‐Saclay Gif‐sur‐Yvette France
3 Centre for Organismal Studies Heidelberg University of Heidelberg Heidelberg Germany
5 Interfaculty Institute of Biochemistry University of Tübingen Tübingen Germany
9 Present address: Institute IMAGINE Paris France
4 Department of Biochemistry Molecular Plant Biology University of Turku Turku Finland
8 Present address: Institute of Microbiology Třeboň Czech Republic
1 Université Paris‐Saclay CEA CNRS Institute for Integrative Biology of the Cell (I2BC) Gif‐sur‐Yvette France
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– name: 8 Present address: Institute of Microbiology Třeboň Czech Republic
– name: 2 Plant Physiology Institute of Plant Biology and Biotechnology University of Muenster Muenster Germany
– name: 4 Department of Biochemistry Molecular Plant Biology University of Turku Turku Finland
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  surname: Mulo
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  organization: Department of Biochemistry, Molecular Plant Biology, University of Turku
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Issue 7
Keywords co‐ and post‐translational modifications
plastid
acetylome
acetyltransferase
quantitative proteomics
Post-translational Modifications & Proteolysis
co-and post-translational modifications
Proteomics
quantitative proteomics Subject Categories Plant Biology
Language English
License Attribution
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These authors contributed equally to this work
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SSID ssj0038182
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Snippet Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and...
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and...
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-a-acetylation (NTA) and...
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation ( NTA )...
Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation...
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SubjectTerms Acetylation
acetylome
Acetyltransferase
Biochemistry, Molecular Biology
Cellular Biology
Chloroplasts
Complexity
co‐ and post‐translational modifications
Deactivation
EMBO30
EMBO31
EMBO56
Enzymatic activity
Enzymes
Genomes
Genomics
In vivo methods and tests
Inactivation
Life Sciences
Localization
Lysine
Mass spectrometry
Mass spectroscopy
Peptides
Phylogenetics
plastid
Plastids
Prokaryotes
Proteins
Quantitative Methods
quantitative proteomics
Selectivity
Structural Biology
Subcellular Processes
Vegetal Biology
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Title Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
URI https://link.springer.com/article/10.15252/msb.20209464
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fmsb.20209464
https://www.proquest.com/docview/2428926077
https://www.proquest.com/docview/2447207812
https://www.proquest.com/docview/2421112190
https://hal.science/hal-02900691
https://pubmed.ncbi.nlm.nih.gov/PMC7339202
https://doaj.org/article/d26b41bab41445bf8117bc4fba9d0b24
Volume 16
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