Acid Phosphatase in Cotyledons of Germinating Vigna mungo Seeds

Tamura, Takeyoshi; Minamikawa, Takao; Koshiba, Tomokazu

doi:10.1093/oxfordjournals.pcp.a076324

Cited by 8 publications

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“…[2][3][4][5][6] These studies demonstrated the presence of multiple PAPases forms in plants, which varied in size and other properties, making their cellular roles difficult to be defined.7) The difficulty in classifying plant PAPase is further compounded by a lack of available sequence information.…”

Section: Introductionmentioning

confidence: 99%

Signal peptide sequence processing site of purple acid phosphatase from kidney bean (Phaseolus vulgaris L. Ohfuku) seeds.

Nakatsuka

Sagane

Kouguchi

et al. 2000

The physico-chemical biology Japanese journal of electrophoresi

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SUMMARYWe purified purple acid phosphatase (PAPase) from kidney bean (Phaseolus vulgaris L. Ohfuku) seeds, a Japanese cultivar of the kidney bean. The molecular mass of the purified native enzyme was estimated approximately 110kDa by gel filtration. Following SDS-PAGE in the presence of 2-mercaptoethanol, glycosylated polypeptides of major 61kDa and minor 59kDa were observed. The N-terminal amino acid sequences for both bands were determined to be GKSSNFVRKTNKNRDMPLDS, suggesting they were two different subunits with the same N-terminal but probably different C-terminal or degree of glycosylation.The partial nucleotide sequences covering the N-terminal region were also determined using polymerase chain reaction (PCR). Comparison with the deduced amino acid sequence from the nucleotide sequence and that of the purified enzyme revealed that the N-terminal amino acid residue corresponded to Gly 23 from the initiation colon (Met). For the deduced amino acid sequence of the PAPase gene, a SignalP (ver. 2.0) analysis program predicted that a 22 amino acid sequence at the N-terminus of a precursor protein was signal peptide. This prediction was in agreement with the fact that PAPase with a signal peptide at the N-terminus was cleaved between Gly 22 and Gly 23 by putative signal peptidase.

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Section: Introductionmentioning

confidence: 99%

Signal peptide sequence processing site of purple acid phosphatase from kidney bean (Phaseolus vulgaris L. Ohfuku) seeds.

Nakatsuka

Sagane

Kouguchi

et al. 2000

The physico-chemical biology Japanese journal of electrophoresi

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“…They are subject to surface denaturation in their pure state and are unstable in diluted solutions (Hye-Shin and Van-Etten 1986), which makes their isolation and purification difficult. In microorganisms, animals and plants, phosphatases, particularly the acidic ones, play an important role in the production and transport of inorganic phosphate, which is essential to a large number of metabolic reactions (Schlosnagle et al 1974, Bieleski andFerguson 1983), Acid phosphatases play a major role in the mobilization of phytate, an organic phosphate reserve in the cotyledon of leguminous seeds, and thus contribute to the growth of the embryonic axes (Sugiura and Sunobe 1962, Mandal and Biswas 1970, Guardiola and Sutcliffe 1971, Tamura et al, 1982, In the present paper we describe a method for the partial purification of a soluble acid phosphatase in Cicer arietinum seeds and report on some of its biochemical properties, prior to the publication of our findings on its physiological involvement in the germination of this seed.…”

Section: Introductionmentioning

confidence: 99%

Partial purification and some biochemical properties of acid phosphatase in germinating chickpea (Cicer arietinum) seeds

Angosto

González

Matilla

1988

Physiologia Plantarum

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An acid phosphatase (EC 3.1.3.2.) from the embryonic axes of chickpea seeds (Cicer arietinum L. cv. Castellana) was purified by ammonium sulphate precipitation, chromatography on Sephacryl S‐200 and polyacrylamide gel electrophoresis. The preparation has an apparent molecular weight of 39 kDa, pH optimum for p‐nitrophenylphosphate hydrolysis of 5.25, and Km of 0.57 mM. The enzyme hydrolyzed all the mono‐ and di‐phosphorylated sugars tested, but had no effect on ATP, ADP, AMP and phosphoenolpyruvate. Phosphate was a competitive inhibitor. Mg2+. Ca2+, Hg2+, Fe3+, arsenate, K+ and Zn2+ were inhibitory. Mn2+, dithiothreitol and EDTA had no effect, and polyamines were activators.

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“…[2][3][4] Enzymes involved in regulatory mechanisms such as protein kinases, protein phosphatases, and mitochondrial enzymes are highly expressed. 3,5,6 The chlorotic cotyledons are similar to other chlorotic counterparts in that both contains lower levels of chlorophyll, thus the photosynthetic activities are not as active. In order to understand the impact of Al on tomato cotyledon development, a comparative proteome analysis was performed using 2D-DIGE following the as previously described procedure.…”

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Aluminum induced proteome changes in tomato cotyledons

Zhou

Sauvé

Thannhauser

2009

Plant Signaling & Behavior

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Cotyledons of tomato seedlings that germinated in a 20 microM AlK(SO(4))(2) solution remained chlorotic while those germinated in an aluminum free medium were normal (green) in color. Previously, we have reported the effect of aluminum toxicity on root proteome in tomato seedlings (Zhou et al.(1)). Two dimensional DIGE protein analysis demonstrated that Al stress affected three major processes in the chlorotic cotyledons: antioxidant and detoxification metabolism (induced), glyoxylate and glycolytic processes (enhanced), and the photosynthetic and carbon fixation machinery (suppressed).

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Acid Phosphatase in Cotyledons of Germinating Vigna mungo Seeds

Cited by 8 publications

References 0 publications

Signal peptide sequence processing site of purple acid phosphatase from kidney bean (Phaseolus vulgaris L. Ohfuku) seeds.

Signal peptide sequence processing site of purple acid phosphatase from kidney bean (Phaseolus vulgaris L. Ohfuku) seeds.

Partial purification and some biochemical properties of acid phosphatase in germinating chickpea (Cicer arietinum) seeds

Aluminum induced proteome changes in tomato cotyledons

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