Distribution of<scp>L</scp>-Azetidine-2-carboxylate<i>N</i>-Acetyltransferase in Yeast

Wada, Masaaki; Okabe, Kae; Kataoka, Michihiko; Shimizu, Sakayu; Yokota, Atsushi; Takagi, Hiroshi

doi:10.1271/bbb.70534

Cited by 19 publications

(13 citation statements)

References 13 publications

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“…Interestingly, Wickerhamia is one of only four ascomycetous genera which are characterised by bi-polar budding (Barnett et al 1990;Kurtzman 2011b), in contrast to the multilateral/multipolar budding observed in C. argentea. Wickerhamia fluorescens possesses the MPR1 gene which confers resistance to the L-proline analogue L-azetidine-2-carboxylate (Wada et al 2008). The MPR1 gene product N-acetyltransferase has also been shown to help scavenge intracellular reactive oxygen species (ROS) and, consequently, increases tolerance to ethanol and freezing stress (Du & Takagi 2005, 2007.…”

Section: Discussionmentioning

confidence: 99%

Candida argentea sp. nov., a copper and silver resistant yeast species

et al. 2011

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Section: Discussionmentioning

confidence: 99%

Candida argentea sp. nov., a copper and silver resistant yeast species

et al. 2011

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“…Based on the structure of Mpr1-CHOP and the predicted binding site of AcCoA on Mpr1, we constructed several Mpr1 mutants with amino acid substitution at positions near CHOP or the acetyl group of AcCoA, both of which are highly conserved among Mpr1 homologs (3,26,27) (Fig. 1C).…”

Section: Resultsmentioning

confidence: 99%

“…Only one base change occurs between MPR1 and MPR2, and the two genes have similar functions. The genes homologous to MPR1 were found in the genomes of many yeasts and fungi, and AZC acetyltransferase activity has already been detected in a number of yeast strains (3), suggesting that the Mpr1 homologs are widely present in yeasts and fungi. However, it is unlikely that AZC is a physiological substrate for Mpr1 because AZC occurs only in certain plants (4)(5)(6).…”

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confidence: 99%

Structural and functional analysis of the yeast N -acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism

Nasuno

Hirano

Itoh

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Mpr1 (sigma1278b gene for proline-analog resistance 1), which was originally isolated as N-acetyltransferase detoxifying the proline analog L-azetidine-2-carboxylate, protects yeast cells from various oxidative stresses. Mpr1 mediates the L-proline and L-arginine metabolism by acetylating L-Δ 1 -pyrroline-5-carboxylate, leading to the L-arginine-dependent production of nitric oxide, which confers oxidative stress tolerance. Mpr1 belongs to the Gcn5-related N-acetyltransferase (GNAT) superfamily, but exhibits poor sequence homology with the GNAT enzymes and unique substrate specificity. Here, we present the X-ray crystal structure of Mpr1 and its complex with the substrate cis-4-hydroxy-L-proline at 1.9 and 2.3 Å resolution, respectively. Mpr1 is folded into α/β-structure with eight-stranded mixed β-sheets and six α-helices. The substrate binds to Asn135 and the backbone amide of Asn172 and Leu173, and the predicted acetyl-CoA-binding site is located near the backbone amide of Phe138 and the side chain of Asn178. Alanine substitution of Asn178, which can interact with the sulfur of acetyl-CoA, caused a large reduction in the apparent k cat value. The replacement of Asn135 led to a remarkable increase in the apparent K m value. These results indicate that Asn178 and Asn135 play an important role in catalysis and substrate recognition, respectively. Such a catalytic mechanism has not been reported in the GNAT proteins. Importantly, the amino acid substitutions in these residues increased the L-Δ 1 -pyrroline-5-carboxylate level in yeast cells exposed to heat stress, indicating that these residues are also crucial for its physiological functions. These studies provide some benefits of Mpr1 applications, such as the breeding of industrial yeasts and the development of antifungal drugs. cyclic amine N-acetyltransferase | X-ray crystallography | reaction mechanism | antioxidant enzyme

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“…The Mpr1 was also reported to protect S. cerevisiae cells from oxidative damage, including H 2 O 2 , heatshock and ethanol stress, by reducing intracellular ROS levels [8]. The MPR1 gene was shown to be widely distributed among various yeast and fungi, but enzymatic analysis of these MPR1 homologs has been limited to S. cerevisiae-complex species and some other genera [16,22,34].…”

Section: Discussionmentioning

confidence: 99%

Heterologous expression of Saccharomyces cerevisiae MPR1 gene confers tolerance to ethanol and l-azetidine-2-carboxylic acid in Hansenula polymorpha

Ishchuk

Abbas

Sibirny

2009

J Ind Microbiol Biotechnol

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Hansenula polymorpha is a naturally xylose-fermenting yeast; however, both its ethanol yield from xylose and ethanol resistance have to be improved before this organism can be used for industrial high-temperature simultaneous saccharification and fermentation of lignocellulosic materials. In the current research, we checked if the expression of the Saccharomyces cerevisiae MPR1 gene encoding N-acetyltransferase can increase the ethanol tolerance of H. polymorpha. The S. cerevisiae MPR1 gene was cloned in the H. polymorpha expression vector under the control of the H. polymorpha strong constitutive promoter of the glyceraldehyde-3-phosphate dehydrogenase gene (GAPDH). H. polymorpha recombinant strains harboring 1-3 copies of the S. cerevisiae MPR1 gene showed enhanced tolerance to L: -azetidine-2-carboxylic acid and ethanol. The obtained results suggest that the expression of the S. cerevisiae MPR1 gene in H. polymorpha can be a useful approach in the construction of H. polymorpha strains with improved ethanol resistance.

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Distribution ofL-Azetidine-2-carboxylateN-Acetyltransferase in Yeast

Cited by 19 publications

References 13 publications

Candida argentea sp. nov., a copper and silver resistant yeast species

Candida argentea sp. nov., a copper and silver resistant yeast species

Structural and functional analysis of the yeast N -acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism

Heterologous expression of Saccharomyces cerevisiae MPR1 gene confers tolerance to ethanol and l-azetidine-2-carboxylic acid in Hansenula polymorpha

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