The Specificity in Vivo of Two Distinct Methionine Aminopeptidases in Saccharomyces cerevisiae

Chen, Shaoping; Vetro, Joseph A.; Chang, Yie Hwa

doi:10.1006/abbi.2001.2675

Cited by 62 publications

(49 citation statements)

References 42 publications

(15 reference statements)

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“…The map1 knockout strain (map1D), however, displays a more severe slow-growth phenotype than the map2D strain [Li and Chang, 1995]. The more severe slow-growth phenotype of yeast map1D correlates well with recent evidence indicating that MetAP1 is primarily responsible for Met init removal in yeast [Chen et al, 2002]. Together, these data suggest that the growth rate of yeast correlates with the level of Met init processing of proteins in vivo.…”

supporting

confidence: 65%

Yeast methionine aminopeptidase type 1 is ribosome‐associated and requires its N‐terminal zinc finger domain for normal function in vivo*

Vetro

Chang

2002

J of Cellular Biochemistry

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Methionine aminopeptidase type 1 (MetAP1) cotranslationally removes N-terminal methionine from nascent polypeptides, when the second residue in the primary structure is small and uncharged. Eukaryotic MetAP1 has an N-terminal zinc finger domain not found in prokaryotic MetAPs. We hypothesized that the zinc finger domain mediates the association of MetAP1 with the ribosomes and have reported genetic evidence that it is important for the normal function of MetAP1 in vivo. In this study, the intracellular role of the zinc finger domain in yeast MetAP1 function was examined. Wild-type MetAP1 expressed in a yeast map1 null strain removed 100% of N-terminal methionine from a reporter protein, while zinc finger mutants removed only 31-35%. Ribosome profiles of map1 null expressing wild-type MetAP1 or one of three zinc finger mutants were compared. Wild-type MetAP1 was found to be an 80S translational complex-associated protein that primarily associates with the 60S subunit. Deletion of the zinc finger domain did not significantly alter the ribosome profile distribution of MetAP1. In contrast, single point mutations in the first or second zinc finger motif disrupted association of MetAP1 with the 60S subunit and the 80S translational complex. Together, these results indicate that the zinc finger domain is essential for the normal processing function of MetAP1 in vivo and suggest that it may be important for the proper functional alignment of MetAP1 on the ribosomes.

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supporting

confidence: 65%

Yeast methionine aminopeptidase type 1 is ribosome‐associated and requires its N‐terminal zinc finger domain for normal function in vivo*

Vetro

Chang

2002

J of Cellular Biochemistry

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“…In this context, retention of the initiator Met in mutants of glutathione-S-transferase expressed in the yeast cytosol or of b-glucuronidase in plants drastically reduces their half-life in vivo (Sawant et al, 2001;Chen et al, 2002). Inhibition of cNME induced by disruption of the PDF gene and/or drug-specific PDF inactivation decreases the steady state levels of PSII D1 and D2 polypeptides and further destabilizes the complex and the whole compartment Both cartoons show the architecture around the thylakoid membranes and the possible interplay between all chloroplastic proteases (Lon, ClpP, Deg, or FtsH) and D1 and D2 at the level of the PSII complex or the ribosome as a function of the NME process (PDF and METAP) and under normal or photoinhibition conditions (referred to as "High Light" in the cartoon).…”

Section: Discussionmentioning

confidence: 99%

Interplay Between N-Terminal Methionine Excision and FtsH Protease Is Essential for Normal Chloroplast Development and Function in Arabidopsis

et al. 2011

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N-terminal methionine excision (NME) is the earliest modification affecting most proteins. All compartments in which protein synthesis occurs contain dedicated NME machinery. Developmental defects induced in Arabidopsis thaliana by NME inhibition are accompanied by increased proteolysis. Although increasing evidence supports a connection between NME and protein degradation, the identity of the proteases involved remains unknown. Here we report that chloroplastic NME (cNME) acts upstream of the FtsH protease complex. Developmental defects and higher sensitivity to photoinhibition associated with the ftsh2 mutation were abolished when cNME was inhibited. Moreover, the accumulation of D1 and D2 proteins of the photosystem II reaction center was always dependent on the prior action of cNME. Under standard light conditions, inhibition of chloroplast translation induced accumulation of correctly NME-processed D1 and D2 in a ftsh2 background, implying that the latter is involved in protein quality control, and that correctly NME-processed D1 and D2 are turned over primarily by the thylakoid FtsH protease complex. By contrast, inhibition of cNME compromises the specific N-terminal recognition of D1 and D2 by the FtsH complex, whereas the unprocessed forms are recognized by other proteases. Our results highlight the tight functional interplay between NME and the FtsH protease complex in the chloroplast.

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“…If the two enzymes have similar specific activities in vivo, cleavage efficiency is likely to be increased. However, this does not appear to be the case in yeast in which MAP1 behaves as the most active, major MAP (78). Data on relative MAP expression and regulation are therefore required to complement prediction algorithms.…”

Section: Nme Prediction Of Natural Bacterial Substrates and Recombinamentioning

confidence: 99%

The Proteomics of N-terminal Methionine Cleavage

Frottin

Martinez

Peynot

et al. 2006

Molecular & Cellular Proteomics

345

350

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The Specificity in Vivo of Two Distinct Methionine Aminopeptidases in Saccharomyces cerevisiae

Cited by 62 publications

References 42 publications

Yeast methionine aminopeptidase type 1 is ribosome‐associated and requires its N‐terminal zinc finger domain for normal function in vivo*

Yeast methionine aminopeptidase type 1 is ribosome‐associated and requires its N‐terminal zinc finger domain for normal function in vivo*

Interplay Between N-Terminal Methionine Excision and FtsH Protease Is Essential for Normal Chloroplast Development and Function in Arabidopsis

The Proteomics of N-terminal Methionine Cleavage

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