Location of Aryl Sulfatase in Conidia and Young Mycelia of
            <i>Neurospora crassa</i>

Scott, Walter A.; Metzenberg, Robert L.

doi:10.1128/jb.104.3.1254-1265.1970

Cited by 36 publications

(15 citation statements)

References 41 publications

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“…Some organisms are able to exploit sources of sulfur other than sulfate, methionine, and cysteine by synthesizing specific sulfatases that cleave sulfate from organic cornpounds or by directly importing other sulfur-containing molecules. Arylsulfatase (Ars), an enzyme that cleaves sulfate frorn aromatic compounds, is synthesized during -S growth by K. aetvgenes (Adachi et al, 1973), A. nidulans (Apte et al, 1974), N. crassa (Scott and Metzenberg, 1970), and C. reinhardtii de Hostos et al, 1988). This periplasmic enzyme enables cells to use aromatic sulfates as a source of sulfur.…”

Section: Introductionmentioning

confidence: 99%

Mutants of Chlamydomonas with Aberrant Responses to Sulfur Deprivation

Davies¹,

Yildiz²,

Grossman³

1994

The Plant Cell

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In the absence of sulfur, Chlamydomonas reinhardtii, a unicellular green alga, increases its rate of sulfate import and synthesizes several periplasmic proteins, including an arylsulfatase (Ars). These changes appear to help cells acclimate to a sulfur-deficient environment. The elevated rate of sulfate import results from an increase in the capacity and affinity of the transport system for sulfate. The synthesis of Ars, a periplasmic enzyme that cleaves sulfate from aromatic compounds, enables cells to use these molecules as a source of sulfur when free sulfate is not available. To characterize the ways in which C. reinhardtii perceives changes in the sulfur status of the environment and regulates its responses to these changes, we mutagenized cells and isolated strains exhibiting aberrant accumulation of Ars activity. These mutants were characterized for Ars activity, ars mRNA accumulation, periplasmic protein accumulation, and sulfate transport activity when grown in both sulfur-sufficient and sulfur-deficient conditions. All of the mutants exhibited pleiotropic effects with respect to several of these responses. Strains harboring double mutant combinations were constructed and characterized for Ars activity and ars mRNA accumulation. From the mutant phenotypes, we inferred that both positive and negative regulatory elements were involved in the acclimation process. Both the epistatic relationships among the mutations and the effects of the lesions on the responses of C. reinhardtii to sulfur limitation distinguished these mutants from similar mutants in Neurospora crassa.

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Section: Introductionmentioning

confidence: 99%

Mutants of Chlamydomonas with Aberrant Responses to Sulfur Deprivation

Davies¹,

Yildiz²,

Grossman³

1994

The Plant Cell

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“…On the other hand, in N. crassa, developmental control can supersede physiological control. A 30-fold increase in arylsulfatase activity is observed in germinating conidia irrespective of sulfur availability (Scott and Metzenberg, 1970). We have identified the derepressible arylsulfatase of C. reinhardtii as a periplasmic component, purified it to homogeneity, and elucidated some aspects of its biosynthesis.…”

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confidence: 99%

Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii.

Hostos

Togasaki

Grossman

1988

The Journal of Cell Biology

118

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Abstract. The unicellular green alga Chlamydomonas reinhardtii responds to sulfate deprivation by producing an arylsulfatase (Lien, T., and O. Schreiner. 1975. Biochim. Biophys. Acta. 384:168-179; Schreiner, O., 1975. Biochim. Biophys. Acta. 384:180-193) and by developing the capacity to transport sulfate more rapidly (our unpublished data). The arylsulfatase activity, detectable 3 h after the transfer of the cells to low sulfate medium (~<10 IxM sulfate), is a periplasmic protein released into the culture medium by cw15, a cell wall-less mutant of C. reinhardtii. We have purified the derepressible arylsulfatase to homogeneity and have raised monospecific antibodies to it. The protein monomer (67.6 kD) associates into a dimer, and the enzyme activity shows an alkaline pH optimum and a Km of 0.3 mM for p-nitrophenylsulfate. Studies focused on arylsulfatase biosynthesis demonstrate that it is glycosylated and synthesized as a higher molecular mass precursor. The mature protein contains complex N-linked oligosaccharides and the primary translation product has an apparent molecular mass ",,5 kD larger than the deglycosylated monomer. Since translatable RNA encoding the arylsulfatase can only be detected in cells after sulfate starvation, it is likely that accumulation of the enzyme is regulated at the level of transcription, although posttranscriptional processes may also be involved.

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“…[1][2][3] Despite their occurrence in eukaryotes and prokaryotes, relevance for a variety of key processes (e.g. development, [4][5][6][7][8][9][10] germination, 11 resistance against toxic defense molecules, 12,13 mucin desulfation, [14][15][16] or degradation of mucopolysaccharides 17,18 ) and the occurrence of various diseases as a result of their malfunction (e.g. lysosomal disorders 17,19 ), their mechanism has not been studied in the same detail as that of the related phosphatases.…”

Section: Introductionmentioning

confidence: 99%

Transition State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis byPseudomonas aeruginosaArylsulfatase

Loo

Berry

Boonyuen

et al. 2018

Preprint

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Pseudomonas aeruginosa arylsulfatase (PAS) hydrolyses sulfate and, promiscuously, phosphate monoesters. Enzyme-catalyzed sulfate transfer is crucial to a wide variety of biological processes, but detailed studies of the mechanistic contributions to its catalysis are lacking. We present an investigation based on linear free energy relationships (LFERs) and kinetic isotope effects (KIEs) of PAS and active site mutants that suggest a key role for leaving group (LG) stabilization. In LFERs wild type PAS has a much less negative Brønsted coefficient (β leaving group obs-Enz = -0.33) than the uncatalyzed reaction (β leaving group obs = -1.81). This situation is diminished when cationic active site groups are exchanged for alanine. The considerable degree of bond breaking during the TS is evidenced by an 18 O bridge KIE of 1.0088. LFER and KIE data for several active site mutants point to leaving group stabilization by active-site lysine K375, in cooperation with histidine H211. 15 N KIEs combined with an increased sensitivity to leaving group ability of the sulfatase activity in neat D 2 O (Δβ leaving group H-D = +0.06) suggest that the mechanism for S-O bridge bond fission shifts, with decreasing leaving group ability, from charge compensation via Lewis acid interactions towards direct proton donation. 18 O nonbridge KIEs indicate that the TS for PAScatalyzed sulfate monoester hydrolysis has a significantly more associative character compared to the uncatalyzed reaction, while PAS-catalyzed phosphate monoester hydrolysis does not show this shift. This difference in enzyme-catalyzed TSs appears to be the major factor favoring specificity toward sulfate over phosphate in this promiscuous hydrolase, since other features are either too similar (uncatalyzed TS) or inherently favor phosphate (charge).

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Location of Aryl Sulfatase in Conidia and Young Mycelia of Neurospora crassa

Cited by 36 publications

References 41 publications

Mutants of Chlamydomonas with Aberrant Responses to Sulfur Deprivation

Mutants of Chlamydomonas with Aberrant Responses to Sulfur Deprivation

Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii.

Transition State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis byPseudomonas aeruginosaArylsulfatase

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