Selection and characterization of pectinase-deficient mutants of the vascular wilt pathogen Verticillium albo-atrum

P K Durrands, Richard M Cooper

Research output: Contribution to journalArticle

Abstract

Three putative pectinase-deficient mutants of the vascular parasite Verticillium albo-atrum which produced, 3, 9 and 43% of wild type pectin lyase were isolated on solid selection media specific for polygalacturonase and pectin lyase detection. The mutants (which were identical to the wild type in growth, morphology and sporulation, apart from 34i which grew poorly on pectic polymers) were grown on pectin, host cell walls, galacturonic acid and glucose to determine changes in production and regulation of pectin lyase, polygalacturonase, cellulase (Cx), β-d-galactosidase, β-d-glucosidase and l-leucine arylamidase. Analysis of culture fluids revealed isolate C23 to be defective in secretion of all enzymes and pectin lyase accumulated intracellularly; isolate 34i was unable to utilize galacturonides and was therefore jointly deficient in production of inducible polygalacturonase and pectin lyase. Analysis of isozyme patterns revealed that mutant 24d produced reduced levels of five of the six pectin lyase isozymes.
Original languageEnglish
Pages (from-to)343-362
Number of pages20
JournalPhysiological and Molecular Plant Pathology
Volume32
Issue number3
DOIs
Publication statusPublished - 1988

Fingerprint

Verticillium
pectin lyase
Verticillium albo-atrum
vascular wilt
Polygalacturonase
polygalacturonase
Blood Vessels
mutants
pathogens
Isoenzymes
isozymes
galacturonic acid
beta-Glucosidase
glucosidases
Cellulase
beta-Galactosidase
beta-galactosidase
sporulation
endo-1,4-beta-glucanase
blood vessels

Cite this

Selection and characterization of pectinase-deficient mutants of the vascular wilt pathogen Verticillium albo-atrum. / Durrands, P K; Cooper, Richard M.

In: Physiological and Molecular Plant Pathology, Vol. 32, No. 3, 1988, p. 343-362.

Research output: Contribution to journalArticle

@article{9d043dca94ac49e7b855d7d8b9eb38f1,
title = "Selection and characterization of pectinase-deficient mutants of the vascular wilt pathogen Verticillium albo-atrum",
abstract = "Three putative pectinase-deficient mutants of the vascular parasite Verticillium albo-atrum which produced, 3, 9 and 43{\%} of wild type pectin lyase were isolated on solid selection media specific for polygalacturonase and pectin lyase detection. The mutants (which were identical to the wild type in growth, morphology and sporulation, apart from 34i which grew poorly on pectic polymers) were grown on pectin, host cell walls, galacturonic acid and glucose to determine changes in production and regulation of pectin lyase, polygalacturonase, cellulase (Cx), β-d-galactosidase, β-d-glucosidase and l-leucine arylamidase. Analysis of culture fluids revealed isolate C23 to be defective in secretion of all enzymes and pectin lyase accumulated intracellularly; isolate 34i was unable to utilize galacturonides and was therefore jointly deficient in production of inducible polygalacturonase and pectin lyase. Analysis of isozyme patterns revealed that mutant 24d produced reduced levels of five of the six pectin lyase isozymes.",
author = "Durrands, {P K} and Cooper, {Richard M}",
year = "1988",
doi = "10.1016/S0885-5765(88)80029-8",
language = "English",
volume = "32",
pages = "343--362",
journal = "Physiological and Molecular Plant Pathology",
issn = "0885-5765",
publisher = "Elsevier Academic Press Inc",
number = "3",

}

TY - JOUR

T1 - Selection and characterization of pectinase-deficient mutants of the vascular wilt pathogen Verticillium albo-atrum

AU - Durrands, P K

AU - Cooper, Richard M

PY - 1988

Y1 - 1988

N2 - Three putative pectinase-deficient mutants of the vascular parasite Verticillium albo-atrum which produced, 3, 9 and 43% of wild type pectin lyase were isolated on solid selection media specific for polygalacturonase and pectin lyase detection. The mutants (which were identical to the wild type in growth, morphology and sporulation, apart from 34i which grew poorly on pectic polymers) were grown on pectin, host cell walls, galacturonic acid and glucose to determine changes in production and regulation of pectin lyase, polygalacturonase, cellulase (Cx), β-d-galactosidase, β-d-glucosidase and l-leucine arylamidase. Analysis of culture fluids revealed isolate C23 to be defective in secretion of all enzymes and pectin lyase accumulated intracellularly; isolate 34i was unable to utilize galacturonides and was therefore jointly deficient in production of inducible polygalacturonase and pectin lyase. Analysis of isozyme patterns revealed that mutant 24d produced reduced levels of five of the six pectin lyase isozymes.

AB - Three putative pectinase-deficient mutants of the vascular parasite Verticillium albo-atrum which produced, 3, 9 and 43% of wild type pectin lyase were isolated on solid selection media specific for polygalacturonase and pectin lyase detection. The mutants (which were identical to the wild type in growth, morphology and sporulation, apart from 34i which grew poorly on pectic polymers) were grown on pectin, host cell walls, galacturonic acid and glucose to determine changes in production and regulation of pectin lyase, polygalacturonase, cellulase (Cx), β-d-galactosidase, β-d-glucosidase and l-leucine arylamidase. Analysis of culture fluids revealed isolate C23 to be defective in secretion of all enzymes and pectin lyase accumulated intracellularly; isolate 34i was unable to utilize galacturonides and was therefore jointly deficient in production of inducible polygalacturonase and pectin lyase. Analysis of isozyme patterns revealed that mutant 24d produced reduced levels of five of the six pectin lyase isozymes.

UR - http://dx.doi.org/10.1016/S0885-5765(88)80029-8

U2 - 10.1016/S0885-5765(88)80029-8

DO - 10.1016/S0885-5765(88)80029-8

M3 - Article

VL - 32

SP - 343

EP - 362

JO - Physiological and Molecular Plant Pathology

JF - Physiological and Molecular Plant Pathology

SN - 0885-5765

IS - 3

ER -