Purification and biosynthesis of cottonseed (<i>Gossypium hirsutum</i> L.) catalase

Kunce, Christine M.; Trelease, Richard N.; Turley, Rickie B.

doi:10.1042/bj2510147

Cited by 67 publications

(53 citation statements)

References 38 publications

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“…In the leaf peroxisomes this form is not processed to the fully active form with subunits of 55 kD. However, as in the cotyledons of mustard (22) and cotton (9), the low active 59 kD catalase has not been detected in sunflower cotyledons (22). As discussed previously (3), inactive (or low active) catalase in sunflower cotyledons could be formed by a modification of mature catalase, and the delay of degradation during peroxisome transition (5) would then lead to the accumulation of this inactivated catalase in the peroxisomes.…”

Section: Discussionmentioning

confidence: 99%

Catalase Synthesis and Turnover during Peroxisome Transition in the Cotyledons of Helianthus annuus L.

Eising

Gerhardt²

1989

Plant Physiol.

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Based on measurements of total catalase hematin and the degradation constants of catalase hematin, zero order rate constants for the synthesis of catalase were determined during the development of sunflower cotyledons (Hellanthus annuus L.).Catalase synthesis reached a sharp maximum of about 400 picomoles hematin per day per cotyledon at day 1.5 during the elaboration of glyoxysomes in the dark. During the transition of glyoxysomes to leaf peroxisomes (greening cotyledons, day 2.5 to 5) catalase synthesis was constant at a level of about 30 to 40 picomoles hematin per day per cotyledon. In the cotyledons of seedlings kept in the dark (day 2.5 to 5) catalase synthesis did not exceed 10 picomoles hematin per day per cotyledon. During the peroxisome transition in the light, total catalase hematin was maintained at a high level, whereas total catalase activity rapidly decreased. In continuous darkness, total catalase hematin decreased considerably from a peak at day 2. The results show that both catalase synthesis and catalase degradation are regulated by light. The tumover characteristics of catalase are in accordance with the concept that glyoxysomes are transformed to leaf peroxisomes as described by the one population model and contradict the two population model and the enzyme synthesis changeover model which both postulate de novo formation of the leaf peroxisome population and degradation of the glyoxysome population.Studies on the transition of peroxisomes from glyoxysomal to leafperoxisomal function in greening oil storing cotyledons have given rise to three models (1). The two population model (6, 7) and the "enzyme synthesis changeover" model (14, 15) postulate a breakdown of glyoxysomes and a de novo formation of leaf peroxisomes, whereas the one population model (18) assumes that glyoxysomes are transformed into leaf peroxisomes. In contrast to the two population model, both the enzyme synthesis changeover model and the one population model predict peroxisomes of intermediary character, i.e. organelles containing both glyoxysomal and leaf peroxisomal enzymes during the transition stage. According to the enzyme synthesis changeover model, leaf-type peroxisomes are formed as a consequence of a turnover of the whole organelles, whereas in the one population model individual enzyme turnover within the same organelle leads to a gradual replacement of glyoxysomal by leaf peroxisomal enzymes. ' Supported by grants from the Deutsche Forschungsgemeinschaft and the Gesellschaft zur Forderung der Westfilischen WilhelmsUniversitat.The existence of peroxisomes of intermediary character has been demonstrated recently in immunocytochemical studies (10, 1 1, 17). These results provide strong evidence against the two population model which postulates two independent populations of peroxisomes functioning exclusively as either glyoxysomes or leaf peroxisomes. The question, however, whether individual enzyme turnover or organelle turnover accounts for the formation of the intermediary peroxisomes, could not be de...

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Section: Discussionmentioning

confidence: 99%

Catalase Synthesis and Turnover during Peroxisome Transition in the Cotyledons of Helianthus annuus L.

Eising

Gerhardt²

1989

Plant Physiol.

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“…Triton X-100 was obtained from Sigma, pectolyase Y-23 was purchased from Seishin Pharmaceutical Co. (Tokyo, Japan), and paraformaldehyde was from Ted Pella Inc. (Redding, CA). IgGs in rabbit sera raised to purified cottonseed catalase (26) were affinity-purified with protein A-Sepharose (Amersham Pharmacia Biotech). Monoclonal antibodies to chloramphenicol acetyltransferase (CAT) in mouse hybridoma medium were a gift from S. Subramani (University of California, San Diego, CA).…”

Section: Methodsmentioning

confidence: 99%

The Sorting Signals for Peroxisomal Membrane-bound Ascorbate Peroxidase Are within Its C-terminal Tail

Mullen

Trelease

2000

Journal of Biological Chemistry

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Peroxisomal ascorbate peroxidase (APX) is a carboxyl tail-anchored, type II (N cytosol -C matrix ) integral membrane protein that functions in the regeneration of NAD ؉ in glyoxysomes of germinated oilseeds and protection of peroxisomes in other organisms from toxic H 2 O 2 . Recently we showed that cottonseed peroxisomal APX was sorted post-translationally from the cytosol to peroxisomes via a novel reticular/circular membranous network that was interpreted to be a subdomain of the endoplasmic reticulum (ER), named peroxisomal ER (pER). Here we report on the molecular signals responsible for sorting peroxisomal APX. Deletions or site-specific substitutions of certain amino acid residues within the hydrophilic C-terminal-most eight-amino acid residues (includes a positively charged domain found in most peroxisomal integral membrane-destined proteins) abolished sorting of peroxisomal APX to peroxisomes via pER. However, the C-terminal tail was not sufficient for sorting chloramphenicol acetyltransferase to peroxisomes via pER, whereas the peptide plus most of the immediately adjacent 21-amino acid transmembrane domain (TMD) of peroxisomal APX was sufficient for sorting. Replacement of the peroxisomal APX TMD with an artificial TMD (devoid of putative sorting sequences) plus the peroxisomal APX C-terminal tail also sorted chloramphenicol acetyltransferase to peroxisomes via pER, indicating that the peroxisomal APX TMD does not possess essential sorting information. Instead, the TMD appears to confer the proper context required for the conserved positively charged domain to function within peroxisomal APX as an overlapping pER sorting signal and a membrane peroxisome targeting signal type 2.Peroxisomes are single membrane-bound organelles that do not contain DNA nor protein-synthesizing machinery. Data published thus far indicate that they acquire their nuclearencoded matrix and boundary membrane protein constituents from the cytosol in a regulated, post-translational manner. For instance, proteins destined for the peroxisomal matrix are sorted by at least two evolutionarily conserved targeting signals, the type 1 and type 2 peroxisomal targeting signal (PTS).

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“…We thank David Oliver, Martin Spalding, and Bob Behal for helpful suggestions and assistance with the fast-protein liquid chromatography, Jonathan Wendel for insight into phylogenetics, Dick Trelease for providing anti-catalase sera (Kunce et al, 1988), and the Bessey Microscopy Facility (Iowa State University). …”

Section: Sequence Analysismentioning

confidence: 99%

“…ACL activity was not assayed in the purified mitochondria and peroxisomes. Samples were also subjected to SDS-PAGE and immunoblot analysis with anti-catalase (Kunce et al, 1988), anti-ACLA, anti-ACLB, and streptavidin . Assays and blots were repeated twice with similar results.…”

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confidence: 99%

Molecular Characterization of a Heteromeric ATP-Citrate Lyase That Generates Cytosolic Acetyl-Coenzyme A in Arabidopsis,

Fatland¹,

Ke²,

Anderson³

et al. 2002

Plant Physiology

196

194

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Acetyl-coenzyme A (CoA) is used in the cytosol of plant cells for the synthesis of a diverse set of phytochemicals including waxes, isoprenoids, stilbenes, and flavonoids. The source of cytosolic acetyl-CoA is unclear. We identified two Arabidopsis cDNAs that encode proteins similar to the amino and carboxy portions of human ATP-citrate lyase (ACL). Coexpression of these cDNAs in yeast (Saccharomyces cerevisiae) confers ACL activity, indicating that both the Arabidopsis genes are required for ACL activity. Arabidopsis ACL is a heteromeric enzyme composed of two distinct subunits, ACLA (45 kD) and ACLB (65 kD). The holoprotein has a molecular mass of 500 kD, which corresponds to a heterooctomer with an A 4 B 4 configuration. ACL activity and the ACLA and ACLB polypeptides are located in the cytosol, consistent with the lack of targeting peptides in the ACLA and ACLB sequences. In the Arabidopsis genome, three genes encode for the ACLA subunit (ACLA-1, At1g10670; ACLA-2, At1g60810; and ACLA-3, At1g09430), and two genes encode the ACLB subunit (ACLB-1, At3g06650 and ACLB-2, At5g49460). The ACLA and ACLB mRNAs accumulate in coordinated spatial and temporal patterns during plant development. This complex accumulation pattern is consistent with the predicted physiological needs for cytosolic acetyl-CoA, and is closely coordinated with the accumulation pattern of cytosolic acetyl-CoA carboxylase, an enzyme using cytosolic acetyl-CoA as a substrate. Taken together, these results indicate that ACL, encoded by the ACLA and ACLB genes of Arabidopsis, generates cytosolic acetyl-CoA. The heteromeric organization of this enzyme is common to green plants (including Chlorophyceae, Marchantimorpha, Bryopsida, Pinaceae, monocotyledons, and eudicots), species of fungi, Glaucophytes, Chlamydomonas, and prokaryotes. In contrast, all known animal ACL enzymes have a homomeric structure, indicating that a evolutionary fusion of the ACLA and ACLB genes probably occurred early in the evolutionary history of this kingdom.Acetyl-coenzyme A (CoA) is an intermediate metabolite that is juxtaposed between catabolic and anabolic processes. As the entry point for the tricarboxylic acid (TCA) cycle, acetyl-CoA can be considered the gateway in the oxidation of carbon derived from the catabolism of fatty acids, certain amino acids (e.g. Leu, Ile, Lys, and Trp), and carbohydrates. Furthermore, acetyl-CoA is the intermediate precursor for the biosynthesis of a wide variety of phytochemicals. Because membranes are impermeable to CoA derivatives, it can be inferred that acetyl-CoA is generated in at least four distinct metabolic pools representing the four subcellular compartments where acetyl-CoA metabolism occurs: plastids, mitochondria, peroxisomes, and the cytosol (Fig. 1). Therefore, plants should have distinct acetyl-CoA-generating systems in mitochondria (for the TCA cycle), in plastids (for de novo fatty acid biosynthesis), in peroxisomes (the product of ␤-oxidation of fatty acids), and in the cytosol (for the biosynthesis of isoprenoids, flavo...

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Purification and biosynthesis of cottonseed (Gossypium hirsutum L.) catalase

Cited by 67 publications

References 38 publications

Catalase Synthesis and Turnover during Peroxisome Transition in the Cotyledons of Helianthus annuus L.

Catalase Synthesis and Turnover during Peroxisome Transition in the Cotyledons of Helianthus annuus L.

The Sorting Signals for Peroxisomal Membrane-bound Ascorbate Peroxidase Are within Its C-terminal Tail

Molecular Characterization of a Heteromeric ATP-Citrate Lyase That Generates Cytosolic Acetyl-Coenzyme A in Arabidopsis,

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