Molecular identification and functional characterization of the first Nα‐acetyltransferase in plastids by global acetylome profiling

Dinh, Trinh V.; Bienvenut, Willy V.; Linster, Eric; Feldman‐Salit, Anna; Jung, Vincent; Meinnel, Thierry; Hell, Rüdiger; Giglione, Carmela; Wirtz, Markus

doi:10.1002/pmic.201500025

Cited by 98 publications

(102 citation statements)

References 48 publications

(99 reference statements)

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“…NAA80/NatH differs in that Nt-acetylation of actin occurs posttranslationally since it constitutes the final step of a unique step-by-step mechanism for Nt-maturation. Posttranslational activity is also suggested for the other more recently identified NATs, NAA60/NatF and NAA70/NatG due to their subcellular localization [8,9]. Contrary to the typical NAT, NAA80/NatH appears to be highly selective with actin as the only substrate in vivo in animals, as demonstrated by the lack of actin Nt-acetylation in NAA80 KO cells by COFRADIC analysis [6].…”

Section: Naa80 Acetylates Actin’s N-terminusmentioning

confidence: 96%

Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin

Aksnes

Marie

Arnesen

et al. 2018

Communicative & Integrative Biology

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Actin is the most abundant protein in our cells, and also one of the most studied. Nevertheless, an important modifier of actin, the N-terminal acetyltransferase (NAT) for actin, remained unknown until now. The recent identification of the enzyme that catalyzes actin acetylation, has opened up for functional studies of unacetylated actin using knockout cells. This enzyme, called NAA80 (Nα-acetyltransferase 80) or NatH, belongs to the NAT family of enzymes, which together provides N-terminal acetylation for around 80 % of the human proteome. In many cases, N-terminal acetylation is essential. In the case of actin, the acetyl group that NAA80 attaches to actin plays an important role in actin’s polymerization properties as well as in actin’s function in cell migration.

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Section: Naa80 Acetylates Actin’s N-terminusmentioning

confidence: 96%

Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin

Aksnes

Marie

Arnesen

et al. 2018

Communicative & Integrative Biology

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“…Interestingly Met-retention on chloroplast proteins has previously been linked to protein instability (Giglione et al, 2003), whilst fMet can act as a destabilizing residue in bacteria, and possibly also chloroplasts (Piatkov et al, 2015). Cotranslational and posttranslational Nt-acetylation also occurs on chloroplastic proteins, which appears to enhance protein stability (Bienvenut et al, 2011); recently a nuclear-encoded chloroplast-targeted NAT that probably catalyses this modification has been identified (Dinh et al, 2015). Accumulating evidence points towards a relationship between N-termini and protein stability in plastids.…”

Section: The N-terminus As a Stability Determinant In Plastidsmentioning

confidence: 99%

From start to finish: amino‐terminal protein modifications as degradation signals in plants

et al. 2016

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Summary The amino‐ (N‐) terminus (Nt) of a protein can undergo a diverse array of co‐ and posttranslational modifications. Many of these create degradation signals (N‐degrons) that mediate protein destruction via the N‐end rule pathway of ubiquitin‐mediated proteolysis. In plants, the N‐end rule pathway has emerged as a major system for regulated control of protein stability. Nt‐arginylation‐dependent degradation regulates multiple growth, development and stress responses, and recently identified functions of Nt‐acetylation can also be linked to effects on the in vivo half‐lives of Nt‐acetylated proteins. There is also increasing evidence that N‐termini could act as important protein stability determinants in plastids. Here we review recent advances in our understanding of the relationship between the nature of protein N‐termini, Nt‐processing events and proteolysis in plants.

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“…The majority of proteins in plants and other eukaryotes are N-acetylated, and a NAT-A loss-of-function Arabidopsis mutant showed pleiotropic developmental and growth defects in Arabidopsis (Ferrández-Ayela et al, 2013), whereas loss of function of NAT-C showed reduced plant growth and photosynthetic capacity (Pesaresi et al, 2003). A chloroplast NAT enzyme (AtNAA70) was recently identified in Arabidopsis and showed N-a-acetylation when expressed in Escherichia coli, in particular for Met, Ala, Thr, and Ser (Dinh et al, 2015). Comparing this specificity with in vivo Arabidopsis chloroplast N-terminome data (Zybailov et al, 2008) suggests that additional NATs operate in chloroplasts (Dinh et al, 2015).…”

Section: N-terminal Acetylationmentioning

confidence: 99%

“…A chloroplast NAT enzyme (AtNAA70) was recently identified in Arabidopsis and showed N-a-acetylation when expressed in Escherichia coli, in particular for Met, Ala, Thr, and Ser (Dinh et al, 2015). Comparing this specificity with in vivo Arabidopsis chloroplast N-terminome data (Zybailov et al, 2008) suggests that additional NATs operate in chloroplasts (Dinh et al, 2015). Because the majority of proteins undergo N-terminal acetylation, it is unclear to what extent this PTM is really regulated (Starheim et al, 2012).…”

Section: N-terminal Acetylationmentioning

confidence: 99%

Update: Post-translational protein modifications in plant metabolism

2015

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ORCID ID: 0000-0001-9536-0487 (K.J.v.W.).Posttranslational modifications (PTMs) of proteins greatly expand proteome diversity, increase functionality, and allow for rapid responses, all at relatively low costs for the cell. PTMs play key roles in plants through their impact on signaling, gene expression, protein stability and interactions, and enzyme kinetics. Following a brief discussion of the experimental and bioinformatics challenges of PTM identification, localization, and quantification (occupancy), a concise overview is provided of the major PTMs and their (potential) functional consequences in plants, with emphasis on plant metabolism. Classic examples that illustrate the regulation of plant metabolic enzymes and pathways by PTMs and their cross talk are summarized. Recent large-scale proteomics studies mapped many PTMs to a wide range of metabolic functions. Unraveling of the PTM code, i.e. a predictive understanding of the (combinatorial) consequences of PTMs, is needed to convert this growing wealth of data into an understanding of plant metabolic regulation.The primary amino acid sequence of proteins is defined by the translated mRNA, often followed by Nor C-terminal cleavages for preprocessing, maturation, and/or activation. Proteins can undergo further reversible or irreversible posttranslational modifications (PTMs) of specific amino acid residues. Proteins are directly responsible for the production of plant metabolites because they act as enzymes or as regulators of enzymes. Ultimately, most proteins in a plant cell can affect plant metabolism (e.g. through effects on plant gene expression, cell fate and development, structural support, transport, etc.). Many metabolic enzymes and their regulators undergo a variety of PTMs, possibly resulting in changes in oligomeric state, stabilization/degradation, and (de)activation (Huber and Hardin, 2004), and PTMs can facilitate the optimization of metabolic flux. However, the direct in vivo consequence of a PTM on a metabolic enzyme or pathway is frequently not very clear, in part because it requires measurements of input and output of the reactions, including flux through the enzyme or pathway. This Update will start out with a short overview on the major PTMs observed for each amino acid residue (Table I), followed by a brief discussion of techniques for the characterization of protein PTMs, including determination of the localization within proteins (i.e. the specific residues) and occupancy. Challenges in dealing with multiple PTMs per protein and cross talk between PTMs will be briefly outlined. We then describe the major physiological PTMs observed in plants as well as PTMs that are nonenzymatically induced during sample preparation (Table II). Finally, this Update is completed with a number of well-studied, classical examples of the regulation of plant metabolism by PTMs, in particular for enzymes in primary metabolism (Calvin cycle, glycolysis, and respiration) and the C4 shuttle accommodating photosynthesis in C4 plants (Table III). As will be ev...

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Molecular identification and functional characterization of the first Nα‐acetyltransferase in plastids by global acetylome profiling

Cited by 98 publications

References 48 publications

Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin

Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin

From start to finish: amino‐terminal protein modifications as degradation signals in plants

Update: Post-translational protein modifications in plant metabolism

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