Utilization of cutin by a pseudomonad isolated from soil

Hankin, Lester; Kolattukudy, P. E.

doi:10.1007/bf01372808

Cited by 22 publications

(6 citation statements)

References 10 publications

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“…Although residual cutin has been found even in ancient sedi ments Palmer, 1976), a cutin-degrading bacterial species has been isolated from soil (Hankin and Kolattukudy, 1971), but the biochemical steps involved in this degradation have not been elucidated. Although residual cutin has been found even in ancient sedi ments Palmer, 1976), a cutin-degrading bacterial species has been isolated from soil (Hankin and Kolattukudy, 1971), but the biochemical steps involved in this degradation have not been elucidated.…”

Section: / Bacterial and Mammalian Degradationmentioning

confidence: 99%

Cutin, Suberin, and Waxes

Kolattukudy¹

1980

Lipids: Structure and Function

160

130

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Section: / Bacterial and Mammalian Degradationmentioning

confidence: 99%

Cutin, Suberin, and Waxes

Kolattukudy¹

1980

Lipids: Structure and Function

160

130

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“…In support of such a hypothesis is the observation that cellulase is induced by cellobiose and derivatives (19). During recent years it was found that several phytopathogenic fungi grow on cutin, the biopolyester made of hydroxy and epoxy fatty acids (7), as the sole source of carbon (4,5,16,22). Under such growth conditions, Fusarium solani f. sp.…”

mentioning

confidence: 99%

Induction of a Biopolyester Hydrolase (Cutinase) by Low Levels of Cutin Monomers in Fusarium solani f. sp. pisi

1978

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Cutin hydrolysate induced the production of an extracellular cutinase by glucose-grown Fusarium solani f. sp. pisi. The rate of production depended on the amount of cutin hydrolysate added up to 80 ,ug/ml, and saturation was attained at this level. Glucose was found to be a repressor of cutinase production. A radial immunodiffusion assay for cutinase was developed, and the induction of cutinase by cutin hydrolysate was confirmed by this direct assay. When cutinase was induced by cutin hydrolysate, exogenous labeled phenylalanine was incorporated into cutinase, which was shown to be the major (>70%) protein in the extracellular fluid. Induction of cutinase by cutin hydrolysate was not inhibited by actinomycin D and was stimulated (=100%) by cordycepin. Addition of cycloheximide with the inducer, or up to 12 h after the addition of the inducer, resulted in a nearly immediate cessation of cutinase production. Deoxyglucose, an inhibitor of proten glycosylation, inhibited the induction of cutinase by cutin hydrolysate. w-Hydroxy fatty acids were more effective in inducing cutinase than any of the other more polar acids of cutin. Experiments with derivatives and analogues of o-hydroxy C16 acid indicated that a free hydroxyl group at the wposition was the most important factor determining the cutinase-inducing activity. n-Aliphatic primary alcohols with 14 or more carbon atoms induced cutinase, and n-C16 was the most effective inducer. These results strongly suggest that the monomers function as the chemical signal which induces the extracellular hydrolase.

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“…Recent electron microscopic studies indicate that enzymatic degradation of cutin may be involved in fungal penetration into the plant (McKeen, 1974), although there is no conclusive evidence for such an enzymatic penetration. Some microorganisms, including plant pathogens, have been shown to live on cutin as their sole carbon source (Heinen and DeVries, 1966;Hankin andKolattukudy, 1971, Purdy andKolattukudy, 1973), and suggestive evidence for the production of cutinolytic enzymes by pathogens has been presented (Shishiyama et al, 1970;Heinen, 1960;Linskens and Haage, 1963).…”

mentioning

confidence: 99%

Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi

Re¹,

Pe²

1975

Biochemistry

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149

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The extracellular fluid of the plant pathogen, Fusarium solani f. pisi, grown on the plant cuticular polymer, cutin, was shown to contain cutinase and p-nitrophenyl palmitate hydrolase activities (R.E. Purdy and P.E. Kolattukudy (1973), Arch. Biochem. Biophys. 159, 61). From this extracellular fluid two isozymes of cutinase and a nonspecific esterase (p-nitrophenyl palmitate hydrolase) were isolated using Sephedex G-100 gel filtration, QAE-Sephadex chromatography, and SE-Sephedex chromatography. Phenolics contained in the extracellular fluid were found to be associated with the cutinase but not with the nonspecific esterase, and the phenolic materials were removed from cutinase at the QAE-Sephedex step. A 34-fold purification of the nonspecific esterase and a 6.5-fold purification of cutinase were achieved by the procedure described. The two isozymes of cutinase (I and II) and the nonspecific esterase were homogeneous as judged by polyacrylamide disc gel electrophoresis and sedimentation equilibrium centrifugation. Molecular weights of cutinase I, cutinase II, and the nonspecific esterase were determined by Sephedex G-100 gel filtration, sedimentation equilibrium centrifugation, amino acid composition, and sodium dodecyl sulfate polyacrylamide disc gel electrophoresis. The values obtained with these techniques agreed with each other and were about 22,000 for both cutinases and 52,000 for the nonspecific esterase. The dodecyl sulfate gel electrophoresis indicated that a small portion of cutinase II contained proteolylic clips, near the middle of the polypeptide chain, and that the nonspecific esterase might also have undergone some proteolylic modification. The amino acid composition of cutinase I was similar to that of cutinase II except for the presence of a larger number of tryptophan residues in the latter, while the amino acid composition of the nonspecific esterase showed more differences from that of either cutinase.

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Utilization of cutin by a pseudomonad isolated from soil

Cited by 22 publications

References 10 publications

Cutin, Suberin, and Waxes

Cutin, Suberin, and Waxes

Induction of a Biopolyester Hydrolase (Cutinase) by Low Levels of Cutin Monomers in Fusarium solani f. sp. pisi

Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi

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