Purification and Characterization of 4-Hydroxyphenylpyruvate Dioxygenase from Maize

Barta, István C.; Böger, Peter

doi:10.1002/(sici)1096-9063(199610)48:2<109::aid-ps447>3.0.co;2-7

Cited by 21 publications

(7 citation statements)

References 9 publications

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“…These optima are similar to the optima found in other HPPDs from different origins (Lindblad et al. 1977, Barta and Boger 1996, García et al. 1997, Kim and Petersen 2002).…”

Section: Resultssupporting

confidence: 86%

FUNCTIONAL CHARACTERIZATION AND EXPRESSION ANALYSIS OFp-HYDROXYPHENYLPYRUVATE DIOXYGENASE FROM THE GREEN ALGACHLAMYDOMONAS REINHARDTII(CHLOROPHYTA)

Gálvez‐Valdivieso

Pineda

Aguilar³

2010

Journal of Phycology

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The enzyme p-hydroxyphenylpyruvate dioxygenase (HPPD) is very important in prenylquinone biosynthesis in all photosynthetic organisms. In this study, we present the functional characterization and expression analysis of HPPD from the unicellular green alga Chlamydomonas reinhardtii P. A. Dang. Recombinant HPPD1 enzyme was purified and characterized. Kinetic analysis revealed a K m of 49 lM for p-hydroxyphenylpyruvate, similar to other HPPDs. The size of HPPD subunit was estimated as 47 kDa by SDS-PAGE, in accordance with the predicted molecular size after HPPD1 cDNA sequence. However, native HPPD1 enzyme showed an apparent molecular mass of 188 kDa and a homotetrameric structure, which suggests a reconsideration of the idea that all eukaryotic HPPDs have a homodimeric structure while all prokaryotic HPPDs are homotetramers. Expression analysis by Northern blot revealed that hppd1 expression is strongly up-regulated by low temperature and poorly regulated by high temperature, darkness, or moderate light changes, suggesting that Chlamydomonas HPPD may play an important role in the synthesis of tocopherols and ⁄ or plastoquinones under stress conditions in the physiological context of the adaptation to growth at low temperatures.

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“…These optima are similar to the optima found in other HPPDs from different origins (Lindblad et al. 1977, Barta and Boger 1996, García et al. 1997, Kim and Petersen 2002).…”

Section: Resultssupporting

confidence: 86%

FUNCTIONAL CHARACTERIZATION AND EXPRESSION ANALYSIS OFp-HYDROXYPHENYLPYRUVATE DIOXYGENASE FROM THE GREEN ALGACHLAMYDOMONAS REINHARDTII(CHLOROPHYTA)

Gálvez‐Valdivieso

Pineda

Aguilar³

2010

Journal of Phycology

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“…To our knowledge this is the first molecular characterization of a plant HPPD. During the preparation of this manuscript a report appeared describing the partial purification of maize HPPD [31]. In contrast with our observations that the carrot HPPD is a homodimer of 48 kDa subunits, which in this respect resembles the mammalian HPPD, the maize HPPD activity was reported to co-elute with a monomeric protein of 43 kDa.…”

Section: Figure 7 Amino Acid Sequence Comparison Between Hppds Of Difcontrasting

confidence: 93%

Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

Garcia¹,

Rodgers²,

Lenne³

et al. 1997

Biochemical Journal

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p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.

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“…Benzobicyclon은 prenylquinone 생합성 경로의 phydroxyphenylpyruvate dehydrogenase (HPPD) 효소를 억제 하여 plastoquinone 및 alpha-tocoperol의 생합성을 저해하 며, 결과적으로 신엽의 백화현상을 일으켜 식물체를 고사 시킨다 (Barta and Böger, 1996;Garcia et al, 1999;Lee et al, 1997;Pallett et al, 1997). …”

Section: 서 론unclassified

“…시킨다 (Barta and Böger, 1996;Garcia et al, 1999;Lee et al, 1997;Pallett et al, 1997). (Han et al, 2009;Im et al, 2007;Im et al, 2008), 약해 정도도 일반형보다 통일형 품종에서 심한 것 으로 보고되었다 (Kim et al, 2012;Kwon et al, 2012).…”

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Phytotoxicity of Whole Crop Forage Rice to Benzobicyclon

양운호¹,

손지영²,

김준환³

et al. 2014

Weed & Turfgrass Science

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Purification and Characterization of 4-Hydroxyphenylpyruvate Dioxygenase from Maize

Cited by 21 publications

References 9 publications

FUNCTIONAL CHARACTERIZATION AND EXPRESSION ANALYSIS OFp-HYDROXYPHENYLPYRUVATE DIOXYGENASE FROM THE GREEN ALGACHLAMYDOMONAS REINHARDTII(CHLOROPHYTA)

FUNCTIONAL CHARACTERIZATION AND EXPRESSION ANALYSIS OFp-HYDROXYPHENYLPYRUVATE DIOXYGENASE FROM THE GREEN ALGACHLAMYDOMONAS REINHARDTII(CHLOROPHYTA)

Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

Phytotoxicity of Whole Crop Forage Rice to Benzobicyclon

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