Adenosine 5′-Triphosphate-Sulfurylase in Corn Roots and Its Partial Purification

Onajobi, Funmilayo D.; Cole, C. V.; Ross, Cleon W.

doi:10.1104/pp.52.6.580

Cited by 22 publications

(8 citation statements)

References 25 publications

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“…The whole leaf activities here are in close agreement with rates reported previously for high plants based on molybdolysis (1, 2),35so42-incorporation into APS (18), and the bioluminescence assay for ATP (5 Figure 2, ratios of 70: 1 and 920: 1 are obtained; or if the whole leaf PEP carboxylase activity is compared with the ATP sulfurylase activity in Table II, a ratio of 324:1 is calculated. In a broad sense, plants contain several hundred-fold more carbon than sulfur.…”

Section: Discussionsupporting

confidence: 75%

Sulfur Assimilation in C₄ Plants

Gerwick¹,

Black²

1979

Plant Physiol.

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The activity of adenosine 5' triphosphate sulfurylase was determined in crabgrass mesophyll cells, bundle sheath strands, and whole leaf extracts. The enzyme was assayed by following molybdate-dependent pyrophosphate release from ATP, 35So42-incorporation into adenosine 5' phosphosulfate, and ATP synthesis dependent upon adenosine 5' phosphosulfate and inorganic pyrophosphate. With all assays, greater than 90% of the activity was found in extracts from bundle sheath strands. The activities in whole leaf extracts were consistently intermediate between the activities of mesophyll and bundle sheath extracts and extract-mixing experiments gave no indication of enzyme activation or inhibition in vitro. Whole leaf activities were several hundred-fold less than concurrent measurements of ribulose 1,5-bisphosphate and phosphoenolpyruvate carboxylase activities, which is interpreted as being consistent with the relative amounts of elemental carbon and sulfur found in higher plants. A hypothesis is presented for the intercellular compartmentation of sulfur assinilation in relationship to N03-and CO2 assimilation in leaves of C4 plants.Higher plants assimilate the essential elements carbon, nitrogen, and sulfur, primarily as the oxides C02, NO3-, and s042-. The transformations of these oxides into organic molecules are coupled to light-dependent reduction and ATP synthesis reactions in leaves. In plants with the C4 pathway of CO2 assimilation, the transformation of CO2 and NO3 is compartmentalized into specific cell types. While atmospheric CO2 initially is fixed into organic acids in the mesophyll cells of C4 plants, the carboxylation of CO2 to form 3-PGA3 occurs exclusively in the bundle sheath cells (6). Conversely N03-, which is made available to the chlorenchyma cells of plants by way of the transpiration stream, moves past the bundle sheath cells of C4 plants and is reduced exclusively in the mesophyll cells (7,17). The cellular compartmentation of carbon-and nitrogen-assimilating enzymes is a primary factor contributing to high rates of carbon assimilation (6) and nitrogen use efficiency (7,9,17) . In some instances the tissue slices were preincubated in 1% pectinase and 1% cellulysin to increase the yield of cell types. The procedure followed was that described by Chen et al. (11) In a control to correct for nonspecific ATPase activity, NaCl was used in place of Na2MoO4. After incubation for timed periods at 37 C, the reaction was stopped-by the addition of 0.5 ml of ice cold 15% trichloroacetic acid. The reaction tubes were transferred to ice. The tubes were centrifuged at 3,000g for 10 min at 4 C and an aliquot (generally 0.4 ml) was removed for Pi determination.

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Section: Discussionsupporting

confidence: 75%

Sulfur Assimilation in C₄ Plants

Gerwick¹,

Black²

1979

Plant Physiol.

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“…In recent years, rapidly expanding work on the subject has confirmed the true metabolic character of the uptake step, showing also its suitability to a genetic and environment regulation (10). Furthermore, the close connection between uptake and successive metabolic events has supported the hypothesis of a common regulation mechanism, as in the classic lactose operon (6).In the present work S042-ion was chosen as the substrate of both a transport and a metabolic step, the latter consisting in the synthesis of the energy-rich compound adenosine 5'-phosphosulfate from ATP and S042- (8). The first step is mediated by proteins making up the S042-transport system (9), the second by the enzyme-protein ATP-sulfurylase (ATP sulfate adenylyl transferase EC 2.7.7.4).…”

mentioning

confidence: 99%

“…In the present work S042-ion was chosen as the substrate of both a transport and a metabolic step, the latter consisting in the synthesis of the energy-rich compound adenosine 5'-phosphosulfate from ATP and S042- (8). The first step is mediated by proteins making up the S042-transport system (9), the second by the enzyme-protein ATP-sulfurylase (ATP sulfate adenylyl transferase EC 2.7.7.4).…”

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confidence: 99%

Development of Sulfate Uptake Capacity and ATP-Sulfurylase Activity during Root Elongation in Maize

Cacco¹,

Saccomani²,

Ferrari³

1977

Plant Physiol.

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Sulfate uptake capacity and ATP-sulfurylase activity were determined in maize roots (Zea mays L. var. XL 363 and mutant XL 363 o2) at increasing root length. The pattern of uptake showed a close similarity to that of ATP-sulfurylase, both activities reaching the maximum level at 9 and 10 cm root length in the XL 363 and XL 363 o2 hybrids, respectively. In addition to the shift of the maximum, opaque-2 mutation caused an enhancement of the two activities at root length below and above the activity peak. The kinetic parameter of uptake, Km, showed a maximum at 3 to 4 and a minimum at 7 to 8 cm. The isoenzyme pattern of ATP-sulfurylase was the same in the two hybrids and did not change with root elongation. A common regulatory mechanism is postulated for uptake and activation of sulfate. The kinetic behavior is interpreted as an index of flexibility of the transport system toward different nutrient status of the environment.The physiological events considered in this study occur just after the germination process, defined as the forcing of the radicle through the seed (4). They pertain to that phase of plant differentiation characterized by the development of a fully operating root system. During this period roots display the most important effort of adaptation to the soil environment: the metabolic factory undergoes a deep modification from a substantially self-supporting matter and energy provision, to a condition requiring an intense exchange with the external world. The two main features of this new metabolic state are: (a) the appearance of transport systems enabling roots to pump nutrients selectively against an electrochemical gradient; (b) the establishment of new metabolic pathways allowing the utilization ot low energy materials, such as inorganic ions, for the de novo synthesis of organic constituents of the living system. Ion uptake has long been underestimated as a factor of plant productivity with respect to the proper metabolic steps. In recent years, rapidly expanding work on the subject has confirmed the true metabolic character of the uptake step, showing also its suitability to a genetic and environment regulation (10). Furthermore, the close connection between uptake and successive metabolic events has supported the hypothesis of a common regulation mechanism, as in the classic lactose operon (6).In the present work S042-ion was chosen as the substrate of both a transport and a metabolic step, the latter consisting in the synthesis of the energy-rich compound adenosine 5'-phosphosulfate from ATP and S042- (8). The first step is mediated by proteins making up the S042-transport system (9), the second by the enzyme-protein ATP-sulfurylase (ATP sulfate adenylyl transferase EC 2.7.7.4). A connection between the ' Support for this research was provided by the Consiglio Nazionale delle Ricerche. two catalytic systems at the level of genetic control was the main assumption of this work, whose objectives were: to verify whether a parallelism exists between the development of SO42-uptake capacity...

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“…The molecular mass of ATP sulfurylase activity in eukaryotic organisms varies from 42 (corn roots) to 800 kD (rat liver enzyme), and the enzyme can be either multimeric or monomeric (Onajobi et al, 1973;Osslund et al, 1982;Yu et al, 1989). The enzyme from Penicillium chrysogenum is an oligomer of 420 kD that is composed of identical or very similar subunits, each with a molecular mass of 69 kD (Martin et al, 1989;Renosto et al, 1990;Foster et al, 1994).…”

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Sulfur Availability and the SAC1 Gene Control Adenosine Triphosphate Sulfurylase Gene Expression in Chlamydomonas reinhardtii

1996

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A Chlamydomonas reinhardtii adenosine triphosphate (ATP) sulfurylase cDNA clone (pATS1) was selected by complementing a mutation in the ATP sulfurylase gene (cysD) of Escherichia coli.E. coli cysD strains harboring pATSl grow on medium containing sulfate as the sole sulfur source and exhibit ATP sulfurylase activity. The amino acid sequence of the C. reinhardtii ATP sulfurylase, derived from the nucleotide sequence of the complementing gene ( A T H ) , is 25 to 40% identical to that of ATP sulfurylases in other eukaryotic organisms and has a putative transit peptide at its amino terminus. ATP sulfurylase mRNA was present when cells were grown in sulfur-replete medium, but accumulated to higher levels when the cells were exposed to sulfur-limiting conditions. Furthermore, sulfur-stress-induced accumulation of the ATSl transcript was reduced in a strain defective in SAC7, a gene that is critical for acclimation to sulfur-limited growth.

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Adenosine 5′-Triphosphate-Sulfurylase in Corn Roots and Its Partial Purification

Cited by 22 publications

References 25 publications

Sulfur Assimilation in C₄ Plants

Sulfur Assimilation in C₄ Plants

Development of Sulfate Uptake Capacity and ATP-Sulfurylase Activity during Root Elongation in Maize

Sulfur Availability and the SAC1 Gene Control Adenosine Triphosphate Sulfurylase Gene Expression in Chlamydomonas reinhardtii

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Adenosine 5′-Triphosphate-Sulfurylase in Corn Roots and Its Partial Purification

Cited by 22 publications

References 25 publications

Sulfur Assimilation in C4 Plants

Sulfur Assimilation in C4 Plants

Development of Sulfate Uptake Capacity and ATP-Sulfurylase Activity during Root Elongation in Maize

Sulfur Availability and the SAC1 Gene Control Adenosine Triphosphate Sulfurylase Gene Expression in Chlamydomonas reinhardtii

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Sulfur Assimilation in C₄ Plants

Sulfur Assimilation in C₄ Plants